Cytoskeletal changes in diseases of the nervous system

doi:10.1007/s11515-014-1290-6

Front. Biol.

2014, Vol. 9

Issue (1) : 5-17 https://doi.org/10.1007/s11515-014-1290-6

REVIEW

Cytoskeletal changes in diseases of the nervous system

Alexandra K. SUCHOWERSKA,Thomas FATH(

)

Neurodegeneration and Repair Unit, School of Medical Sciences, University of New South Wales, Randwick, New South Wales 2052, Australia

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Abstract

The neuronal cytoskeleton not only provides the structural backbone of neurons, but also plays a fundamental role in maintaining neuronal functions. Dysregulation of neuronal architecture is evident in both injury and diseases of the central nervous system. These changes often result in the disruption of protein trafficking, loss of synapses and the death of neurons, ultimately impacting on signal transmission and manifesting in the disease phenotype. Furthermore, mutations in cytoskeletal proteins have been implicated in numerous diseases and, in some cases, identified as the cause of the disease, highlighting the critical role of the cytoskeleton in disease pathology. This review focuses on the role of cytoskeletal proteins in the pathology of mental disorders, neurodegenerative diseases and motor function deficits. In particular, we illustrate how cytoskeletal proteins can be directly linked to disease pathology and progression.

Keywords nervous system disease cytoskeleton actin microtubules intermediate filaments

Corresponding Author(s): Thomas FATH

Issue Date: 13 May 2014

Cite this article:

Alexandra K. SUCHOWERSKA,Thomas FATH. Cytoskeletal changes in diseases of the nervous system[J]. Front. Biol., 2014, 9(1): 5-17.

URL:

https://academic.hep.com.cn/fib/EN/10.1007/s11515-014-1290-6
https://academic.hep.com.cn/fib/EN/Y2014/V9/I1/5

Fig.1 Cellular architectural changes due to disease or after injury in developing neurons (A), mature neurons in the central nervous system (B) and motor neurons (C). Post mortem studies in schizophrenia patients reveal upregulation of microtubule associated protein (MAP) 2 and 6 in the prefrontal cortex (Anderson et al., 1996 [2], Cotter et al., 2000 [3], Shimizu et al., 2006 [4]). Schizophrenia patients are also associated with up regulation of two isoforms of neurofilaments (NFs), NF-L and NF-M, which is suggested to impact on NMDA receptor localisation to the post synaptic density (Clinton et al., 2003[13], Clinton et al., 2004[14], Ehlers et al., 1995[15], Ehlers et al., 1998[16]). Reductions in phosphorylated cofilin and filamentous actin are shown in dendritic spines in mouse models of schizophrenia (Asrar et al., 2009[17]). Epileptic patients have reduced levels of phosphorylated MAP2 associated with decreased cytoskeletal stability (Sanchez et al., 2001[10]). Increase activation of cofilin, and subsequent reduction in actin stabilisation is observed in epilepsy (Chai et al., 2009[6]). Mutations in the Parkinson’s disease associated protein alpha-synuclein, have been associated with increases in the rate of actin polymerisation (Sousa et al., 2009[5]). Accumulation of filamentous actin and actin-associated proteins into rod shaped inclusions termed Hirano bodies are observed in Alzheimer’s disease (Galloway et al., 1987[1]). The MAP tau is known to aggregate into neurofibrillary tangles and neuropil threads within neurons in Alzheimer’s Disease (Goedert et al., 1988[9]). The accumulation of tau also inhibits kinesin-driven anterograde transport, impacting on neurodegeneration (Dixit et al., 2008[8]). Mutations in the parkin protein, which is known to bind microtubules, have been linked to autosomal recessive and sporadic forms of Parkinson’s disease (Lucking et al., 2000 [11], Scott et al., 2001 [12]). Mutations in the actin associated protein PFN1 have been identified in familial amyotrophic lateral sclerosis (ALS), with cell culture studies indicating that mutant PFN1 causes decreased bound actin levels, axon outgrowth and growth cone size (Wu et al., 2012[7]). Mouse models of ALS show NF-L only inclusions in the spinal cord of pre-symptomatic mice (Morrison et al., 2000[18]). ALS patients also exhibit aggregation of phosphorylated NFs in the perikarya and proximal axons (Manetto et al., 1988[19], Munoz et al., 1988[20]). Alterations to the normal functioning of NFs in ALS may lead to alterations in microtubule stability due to inhibition of normal NF-MT binding (Bocquet et al., 2009[21]).

Tab.1 Diseases involving the cytoskeleton

1	Al-ChalabiA, AndersenP M, NilssonP, ChiozaB, AnderssonJ L, RussC, ShawC E, PowellJ F, LeighP N (1999). Deletions of the heavy neurofilament subunit tail in amyotrophic lateral sclerosis. Hum Mol Genet, 8(2): 157–164 doi: 10.1093/hmg/8.2.157 pmid: 9931323
2	AndersonS A, VolkD W, LewisD A (1996). Increased density of microtubule associated protein 2-immunoreactive neurons in the prefrontal white matter of schizophrenic subjects. Schizophr Res, 19(2–3): 111–119 doi: 10.1016/0920-9964(96)88521-5 pmid: 8789909
3	AndrianantoandroE, PollardT D (2006). Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell, 24(1): 13–23 doi: 10.1016/j.molcel.2006.08.006 pmid: 17018289
4	AndrieuxA, SalinP A, VernetM, KujalaP, BaratierJ, Gory-FauréS, BoscC, PointuH, ProiettoD, SchweitzerA, DenarierE, KlumpermanJ, JobD (2002). The suppression of brain cold-stable microtubules in mice induces synaptic defects associated with neuroleptic-sensitive behavioral disorders. Genes Dev, 16(18): 2350–2364 doi: 10.1101/gad.223302 pmid: 12231625
5	ArberS, BarbayannisF A, HanserH, SchneiderC, StanyonC A, BernardO, CaroniP (1998). Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature, 393(6687): 805–809 doi: 10.1038/31729 pmid: 9655397
6	ArmstrongR A, CairnsN J (2012). Different molecular pathologies result in similar spatial patterns of cellular inclusions in neurodegenerative disease: a comparative study of eight disorders. J Neural Transm, 119(12): 1551–1560 doi: 10.1007/s00702-012-0838-3 pmid: 22678700
7	ArmstrongR A, KertyE, SkullerudK, CairnsN J (2006). Neuropathological changes in ten cases of neuronal intermediate filament inclusion disease (NIFID): a study using alpha-internexin immunohistochemistry and principal components analysis (PCA). J Neural Transm, 113(9): 1207–1215 doi: 10.1007/s00702-005-0387-0 pmid: 16362634
8	AsburyA K, GaleM K, CoxS C, BaringerJ R, BergB O (1972). Giant axonal neuropathy—a unique case with segmental neurofilamentous masses. Acta Neuropathol, 20(3): 237–247 doi: 10.1007/BF00686905 pmid: 5044004
9	AsrarS, MengY, ZhouZ, TodorovskiZ, HuangW W, JiaZ (2009). Regulation of hippocampal long-term potentiation by p21-activated protein kinase 1 (PAK1). Neuropharmacology, 56(1): 73–80 doi: 10.1016/j.neuropharm.2008.06.055 pmid: 18644395
10	BaasP W, AhmadF J (2013). Beyond taxol: microtubule-based treatment of disease and injury of the nervous system. Brain, 136(Pt 10): 2937–2951 doi: 10.1093/brain/awt153 pmid: 23811322
11	BallatoreC, LeeV M, TrojanowskiJ Q (2007). Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders. Nat Rev Neurosci, 8(9): 663–672 doi: 10.1038/nrn2194 pmid: 17684513
12	BégouM, BrunP, BertrandJ B, JobD, SchweitzerA, D’AmatoT, SaoudM, AndrieuxA, Suaud-ChagnyM F (2007). Post-pubertal emergence of alterations in locomotor activity in stop null mice. Synapse, 61(9): 689–697 doi: 10.1002/syn.20409 pmid: 17559095
13	BégouM, VolleJ, BertrandJ B, BrunP, JobD, SchweitzerA, SaoudM, D’AmatoT, AndrieuxA, Suaud-ChagnyM F (2008). The stop null mice model for schizophrenia displays [corrected] cognitive and social deficits partly alleviated by neuroleptics. Neuroscience, 157(1): 29–39 doi: 10.1016/j.neuroscience.2008.07.080 pmid: 18804150
14	BelichenkoP V, DahlströmA (1995). Studies on the 3-dimensional architecture of dendritic spines and varicosities in human cortex by confocal laser scanning microscopy and Lucifer yellow microinjections. J Neurosci Methods, 57(1): 55–61 doi: 10.1016/0165-0270(94)00125-Z pmid: 7791365
15	Bento-AbreuA, Van DammeP, Van Den BoschL, RobberechtW (2010). The neurobiology of amyotrophic lateral sclerosis. Eur J Neurosci, 31(12): 2247–2265 doi: 10.1111/j.1460-9568.2010.07260.x pmid: 20529130
16	BergeronC, Beric-MaskarelK, MuntasserS, WeyerL, SomervilleM J, PercyM E (1994). Neurofilament light and polyadenylated mRNA levels are decreased in amyotrophic lateral sclerosis motor neurons. J Neuropathol Exp Neurol, 53(3): 221–230 doi: 10.1097/00005072-199405000-00002 pmid: 7909836
17	BernhardtR, MatusA (1984). Light and electron microscopic studies of the distribution of microtubule-associated protein 2 in rat brain: a difference between dendritic and axonal cytoskeletons. J Comp Neurol, 226(2): 203–221 doi: 10.1002/cne.902260205 pmid: 6736300
18	BishopA L, HallA (2000). Rho GTPases and their effector proteins. Biochem J, 348(Pt 2): 241–255 doi: 10.1042/0264-6021:3480241 pmid: 10816416
19	BloomG S, ValleeR B (1983). Association of microtubule-associated protein 2 (MAP 2) with microtubules and intermediate filaments in cultured brain cells. J Cell Biol, 96(6): 1523–1531 doi: 10.1083/jcb.96.6.1523 pmid: 6343400
20	BocquetA, BergesR, FrankR, RobertP, PetersonA C, EyerJ (2009). Neurofilaments bind tubulin and modulate its polymerization. J Neurosci, 29(35): 11043–11054 doi: 10.1523/JNEUROSCI.1924-09.2009 pmid: 19726663
21	BoschM, HayashiY (2012). Structural plasticity of dendritic spines. Curr Opin Neurobiol, 22(3): 383–388 doi: 10.1016/j.conb.2011.09.002 pmid: 21963169
22	BrettschneiderJ, PetzoldA, SüssmuthS D, LudolphA C, TumaniH (2006). Axonal damage markers in cerebrospinal fluid are increased in ALS. Neurology, 66(6): 852–856 doi: 10.1212/01.wnl.0000203120.85850.54 pmid: 16567701
23	BrunP, BégouM, AndrieuxA, Mouly-BadinaL, ClergetM, SchweitzerA, ScarnaH, RenaudB, JobD, Suaud-ChagnyM F (2005). Dopaminergic transmission in STOP null mice. J Neurochem, 94(1): 63–73 doi: 10.1111/j.1471-4159.2005.03166.x pmid: 15953350
24	BrundenK R, ZhangB, CarrollJ, YaoY, PotuzakJ S, HoganA M, IbaM, JamesM J, XieS X, BallatoreC, SmithA B 3rd, LeeV M Y, TrojanowskiJ Q (2010). Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J Neurosci, 30(41): 13861–13866 doi: 10.1523/JNEUROSCI.3059-10.2010 pmid: 20943926
25	BugyiB, PappG, HildG, LõrinczyD, NevalainenE M, LappalainenP, SomogyiB, NyitraiM (2006). Formins regulate actin filament flexibility through long range allosteric interactions. J Biol Chem, 281(16): 10727–10736 doi: 10.1074/jbc.M510252200 pmid: 16490788
26	CaceresA, BankerG, StewardO, BinderL, PayneM (1984). MAP2 is localized to the dendrites of hippocampal neurons which develop in culture. Brain Res, 315(2): 314–318 pmid: 6722593
27	CairnsN J, LeeV M Y, TrojanowskiJ Q (2004). The cytoskeleton in neurodegenerative diseases. J Pathol, 204(4): 438–449 doi: 10.1002/path.1650 pmid: 15495240
28	ChaiX, FörsterE, ZhaoS, BockH H, FrotscherM (2009). Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3. J Neurosci, 29(1): 288–299 doi: 10.1523/JNEUROSCI.2934-08.2009 pmid: 19129405
29	ChenY, ZhengZZ, HuangR, ChenK, SongW, ZhaoB, ChenX, YangY, YuanL, ShangHF (2013) PFN1 mutations are rare in Han Chinese populations with amyotrophic lateral sclerosis. Neurobiol Aging34:1922 e1921–1925.
30	ClintonS M, AbelsonS, HaroutunianV, DavisK, Meador-WoodruffJ H (2004). Neurofilament subunit protein abnormalities in the thalamus in scizophrenia. Thalamus Relat Syst, 2: 265–272
31	ClintonS M, HaroutunianV, DavisK L, Meador-WoodruffJ H (2003). Altered transcript expression of NMDA receptor-associated postsynaptic proteins in the thalamus of subjects with schizophrenia. Am J Psychiatry, 160(6): 1100–1109 doi: 10.1176/appi.ajp.160.6.1100 pmid: 12777268
32	CohenR S, ChungS K, PfaffD W (1985). Immunocytochemical localization of actin in dendritic spines of the cerebral cortex using colloidal gold as a probe. Cell Mol Neurobiol, 5(3): 271–284 doi: 10.1007/BF00711012 pmid: 4064076
33	CollardJ F, CôtéF, JulienJ P (1995). Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis. Nature, 375(6526): 61–64 doi: 10.1038/375061a0 pmid: 7536898
34	CôtéF, CollardJ F, JulienJ P (1993). Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell, 73(1): 35–46 doi: 10.1016/0092-8674(93)90158-M pmid: 8462101
35	CotterD, WilsonS, RobertsE, KerwinR, EverallI P (2000). Increased dendritic MAP2 expression in the hippocampus in schizophrenia. Schizophr Res, 41(2): 313–323 doi: 10.1016/S0920-9964(99)00068-7 pmid: 10708340
36	DaoudH, DobrzenieckaS, CamuW, MeiningerV, DupreN, DionPA, RouleauGA (2013) Mutation analysis of PFN1 in familial amyotrophic lateral sclerosis patients. Neurobiol Aging34:1311 e1311–1312.
37	DehmeltL, HalpainS (2004). Actin and microtubules in neurite initiation: are MAPs the missing link? J Neurobiol, 58(1): 18–33 doi: 10.1002/neu.10284 pmid: 14598367
38	DentE W, KalilK (2001). Axon branching requires interactions between dynamic microtubules and actin filaments. J Neurosci, 21(24): 9757–9769 pmid: 11739584
39	DeoA J, GoldszerI M, LiS, DiBitettoJ V, HenteleffR, SampsonA, LewisD A, PenzesP, SweetR A (2013). PAK1 protein expression in the auditory cortex of schizophrenia subjects. PLoS ONE, 8(4): e59458 doi: 10.1371/journal.pone.0059458 pmid: 23613712
40	Díez-GuerraF J, AvilaJ (1993). MAP2 phosphorylation parallels dendrite arborization in hippocampal neurones in culture. Neuroreport, 4(4): 419–422 doi: 10.1097/00001756-199304000-00020 pmid: 8499602
41	DiProsperoN A, ChenE Y, CharlesV, PlomannM, KordowerJ H, TagleD A (2004). Early changes in Huntington’s disease patient brains involve alterations in cytoskeletal and synaptic elements. J Neurocytol, 33(5): 517–533 doi: 10.1007/s11068-004-0514-8 pmid: 15906159
42	DixitR, RossJ L, GoldmanY E, HolzbaurE L (2008). Differential regulation of dynein and kinesin motor proteins by tau. Science, 319(5866): 1086–1089 doi: 10.1126/science.1152993 pmid: 18202255
43	DomR, MalfroidM, BaroF (1976). Neuropathology of Huntington’s chorea.Studies of the ventrobasal complex of the thalamus. Neurology, 26(1): 64–68 doi: 10.1212/WNL.26.1.64 pmid: 128708
44	DowningK H, NogalesE (1998). Tubulin and microtubule structure. Curr Opin Cell Biol, 10(1): 16–22 doi: 10.1016/S0955-0674(98)80082-3 pmid: 9484591
45	DuanW, GuoY, JiangH, YuX, LiC (2011). MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1. Brain Res, 1397: 1–9 doi: 10.1016/j.brainres.2011.05.006 pmid: 21620381
46	EbnethA, GodemannR, StamerK, IllenbergerS, TrinczekB, MandelkowE (1998). Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer’s disease. J Cell Biol, 143(3): 777–794 doi: 10.1083/jcb.143.3.777 pmid: 9813097
47	EdwardsD C, SandersL C, BokochG M, GillG N (1999). Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol, 1(5): 253–259 doi: 10.1038/12963 pmid: 10559936
48	EhlersM D, FungE T, O’BrienR J, HuganirR L (1998). Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J Neurosci, 18(2): 720–730 pmid: 9425014
49	EhlersM D, TingleyW G, HuganirR L (1995). Regulated subcellular distribution of the NR1 subunit of the NMDA receptor. Science, 269(5231): 1734–1737 doi: 10.1126/science. pmid: 7569904
50	FerriC P, PrinceM, BrayneC, BrodatyH, FratiglioniL, GanguliM, HallK, HasegawaK, HendrieH, HuangY, JormA, MathersC, MenezesP R, RimmerE, ScazufcaM, and the Alzheimer’s Disease International (2005). Global prevalence of dementia: a Delphi consensus study. Lancet, 366(9503): 2112–2117 doi: 10.1016/S0140-6736(05)67889-0 pmid: 16360788
51	FiglewiczD A, KrizusA, MartinoliM G, MeiningerV, DibM, RouleauG A, JulienJ P (1994). Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum Mol Genet, 3(10): 1757–1761 doi: 10.1093/hmg/3.10.1757 pmid: 7849698
52	FreimanT M, Eismann-SchweimlerJ, FrotscherM (2011). Granule cell dispersion in temporal lobe epilepsy is associated with changes in dendritic orientation and spine distribution. Exp Neurol, 229(2): 332–338 doi: 10.1016/j.expneurol.2011.02.017 pmid: 21376037
53	FuchsE, ClevelandD W (1998). A structural scaffolding of intermediate filaments in health and disease. Science, 279(5350): 514–519 doi: 10.1126/science.279.5350.514 pmid: 9438837
54	FulgaT A, Elson-SchwabI, KhuranaV, SteinhilbM L, SpiresT L, HymanB T, FeanyM B (2007). Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol, 9(2): 139–148 doi: 10.1038/ncb1528 pmid: 17187063
55	GallowayP G, MulvihillP, PerryG (1992). Filaments of Lewy bodies contain insoluble cytoskeletal elements. Am J Pathol, 140(4): 809–822 pmid: 1314025
56	GallowayP G, PerryG, GambettiP (1987). Hirano body filaments contain actin and actin-associated proteins. J Neuropathol Exp Neurol, 46(2): 185–199 doi: 10.1097/00005072-198703000-00006 pmid: 3029338
57	GareyL J, OngW Y, PatelT S, KananiM, DavisA, MortimerA M, BarnesT R, HirschS R (1998). Reduced dendritic spine density on cerebral cortical pyramidal neurons in schizophrenia. J Neurol Neurosurg Psychiatry, 65(4): 446–453 doi: 10.1136/jnnp.65.4.446 pmid: 9771764
58	GeW W, WenW, StrongW, Leystra-LantzC, StrongM J (2005). Mutant copper-zinc superoxide dismutase binds to and destabilizes human low molecular weight neurofilament mRNA. J Biol Chem, 280(1): 118–124 pmid: 15507437
59	GibsonP H, TomlinsonB E (1977). Numbers of Hirano bodies in the hippocampus of normal and demented people with Alzheimer’s disease. J Neurol Sci, 33(1–2): 199–206 doi: 10.1016/0022-510X(77)90193-9 pmid: 903782
60	GlantzL A, LewisD A (2000). Decreased dendritic spine density on prefrontal cortical pyramidal neurons in schizophrenia. Arch Gen Psychiatry, 57(1): 65–73 doi: 10.1001/archpsyc.57.1.65 pmid: 10632234
61	GlantzL A, LewisD A (2001). Dendritic spine density in schizophrenia and depression. Arch Gen Psychiatry, 58(2): 203 doi: 10.1001/archpsyc.58.2.203 pmid: 11177126
62	GoedertM, WischikC M, CrowtherR A, WalkerJ E, KlugA (1988). Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc Natl Acad Sci USA, 85(11): 4051–4055 doi: 10.1073/pnas.85.11.4051 pmid: 3131773
63	Grundke-IqbalI, IqbalK, QuinlanM, TungY C, ZaidiM S, WisniewskiH M (1986a). Microtubule-associated protein tau.A component of Alzheimer paired helical filaments. J Biol Chem, 261(13): 6084–6089 pmid: 3084478
64	Grundke-IqbalI, IqbalK, TungY C, QuinlanM, WisniewskiH M, BinderL I (1986b). Abnormal phosphorylation of the microtubule-associated protein tau (τ) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci USA, 83(13): 4913–4917 doi: 10.1073/pnas.83.13.4913 pmid: 3088567
65	GunningP, O’NeillG, HardemanE (2008). Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol Rev, 88(1): 1–35 doi: 10.1152/physrev.00001.2007 pmid: 18195081
66	HaasC A, DudeckO, KirschM, HuszkaC, KannG, PollakS, ZentnerJ, FrotscherM (2002). Role for reelin in the development of granule cell dispersion in temporal lobe epilepsy. J Neurosci, 22(14): 5797–5802 pmid: 12122039
67	HangerD P, AndertonB H, NobleW (2009). Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med, 15(3): 112–119 doi: 10.1016/j.molmed.2009.01.003 pmid: 19246243
68	HayashiM L, ChoiS Y, RaoB S, JungH Y, LeeH K, ZhangD, ChattarjiS, KirkwoodA, TonegawaS (2004). Altered cortical synaptic morphology and impaired memory consolidation in forebrain- specific dominant-negative PAK transgenic mice. Neuron, 42(5): 773–787 doi: 10.1016/j.neuron.2004.05.003 pmid: 15182717
69	HillJ J, HashimotoT, LewisD A (2006). Molecular mechanisms contributing to dendritic spine alterations in the prefrontal cortex of subjects with schizophrenia. Mol Psychiatry, 11(6): 557–566 doi: 10.1038/sj.mp.4001792 pmid: 16402129
70	HillW D, LeeV M, HurtigH I, MurrayJ M, TrojanowskiJ Q (1991). Epitopes located in spatially separate domains of each neurofilament subunit are present in Parkinson’s disease Lewy bodies. J Comp Neurol, 309(1): 150–160 doi: 10.1002/cne.903090111 pmid: 1716646
71	HouserC R (1990). Granule cell dispersion in the dentate gyrus of humans with temporal lobe epilepsy. Brain Res, 535(2): 195–204 doi: 10.1016/0006-8993(90)91601-C pmid: 1705855
72	HuttonM, LendonC L, RizzuP, BakerM, FroelichS, HouldenH, Pickering-BrownS, ChakravertyS, IsaacsA, GroverA, HackettJ, AdamsonJ, LincolnS, DicksonD, DaviesP, PetersenR C, StevensM, de GraaffE, WautersE, van BarenJ, HillebrandM, JoosseM, KwonJ M, NowotnyP, CheL K, NortonJ, MorrisJ C, ReedL A, TrojanowskiJ, BasunH, LannfeltL, NeystatM, FahnS, DarkF, TannenbergT, DoddP R, HaywardN, KwokJ B, SchofieldP R, AndreadisA, SnowdenJ, CraufurdD, NearyD, OwenF, OostraB A, HardyJ, GoateA, van SwietenJ, MannD, LynchT, HeutinkP (1998). Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature, 393(6686): 702–705 doi: 10.1038/31508 pmid: 9641683
73	IngreC, LandersJE, RizikN, VolkAE, AkimotoC, BirveA, HubersA, KeaglePJ, PiotrowskaK, PressR, AndersenPM, LudolphAC, WeishauptJ H (2013). A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts. Neurobiol Aging, 34:1708 e1701–1706
74	IqbalK, Grundke-IqbalI, ZaidiT, MerzP A, WenG Y, ShaikhS S, WisniewskiH M, AlafuzoffI, WinbladB (1986). Defective brain microtubule assembly in Alzheimer’s disease. Lancet, 2(8504): 421–426 doi: 10.1016/S0140-6736(86)92134-3 pmid: 2874414
75	IttnerL M, KeY D, DelerueF, BiM, GladbachA, van EerselJ, WölfingH, ChiengB C, ChristieM J, NapierI A, EckertA, StaufenbielM, HardemanE, GötzJ (2010). Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer’s disease mouse models. Cell, 142(3): 387–397 doi: 10.1016/j.cell.2010.06.036 pmid: 20655099
76	JordanovaA, De JongheP, BoerkoelC F, TakashimaH, De VriendtE, CeuterickC, MartinJ J, ButlerI J, ManciasP, PapasozomenosS Ch, TerespolskyD, PotockiL, BrownC W, ShyM, RitaD A, TournevI, KremenskyI, LupskiJ R, TimmermanV (2003). Mutations in the neurofilament light chain gene (NEFL) cause early onset severe Charcot-Marie-Tooth disease. Brain, 126(Pt 3): 590–597 doi: 10.1093/brain/awg059 pmid: 12566280
77	KeY D, SuchowerskaA K, van der HovenJ, De SilvaD M, WuC W, van EerselJ, IttnerA, IttnerL M (2012). Lessons from tau-deficient mice. Int J Alzheimers Dis, 2012: 873270 doi: 10.1155/2012/873270 pmid: 22720190
78	KimC H, LismanJ E (1999). A role of actin filament in synaptic transmission and long-term potentiation. J Neurosci, 19(11): 4314–4324 pmid: 10341235
79	KorobovaF, SvitkinaT (2008). Arp2/3 complex is important for filopodia formation, growth cone motility, and neuritogenesis in neuronal cells. Mol Biol Cell, 19(4): 1561–1574 doi: 10.1091/mbc.E07-09-0964 pmid: 18256280
80	KrügerR, FischerC, SchulteT, StraussK M, MüllerT, WoitallaD, BergD, HungsM, GobbeleR, BergerK, EpplenJ T, RiessO, SchölsL (2003). Mutation analysis of the neurofilament M gene in Parkinson’s disease. Neurosci Lett, 351(2): 125–129 doi: 10.1016/S0304-3940(03)00903-0 pmid: 14583397
81	KuhnT B, BamburgJ R (2008). Tropomyosin and ADF/cofilin as collaborators and competitors. Adv Exp Med Biol, 644: 232–249 doi: 10.1007/978-0-387-85766-4_18 pmid: 19209826
82	LattanteS, Le BerI, CamuzatA, BriceA, KabashiE (2013). Mutations in the PFN1 gene are not a common cause in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration in France. Neurobiol Aging, 34:1709 e1701–1702
83	LavedanC, BuchholtzS, NussbaumR L, AlbinR L, PolymeropoulosM H (2002). A mutation in the human neurofilament M gene in Parkinson’s disease that suggests a role for the cytoskeleton in neuronal degeneration. Neurosci Lett, 322(1): 57–61 doi: 10.1016/S0304-3940(01)02513-7 pmid: 11958843
84	LeeM K, MarszalekJ R, ClevelandD W (1994). A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease. Neuron, 13(4): 975–988 doi: 10.1016/0896-6273(94)90263-1 pmid: 7946341
85	LeeV M, GoedertM, TrojanowskiJ Q (2001). Neurodegenerative tauopathies. Annu Rev Neurosci, 24(1): 1121–1159 doi: 10.1146/annurev.neuro.24.1.1121 pmid: 11520930
86	LiB, ChohanM O, Grundke-IqbalI, IqbalK (2007). Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau. Acta Neuropathol, 113(5): 501–511 doi: 10.1007/s00401-007-0207-8 pmid: 17372746
87	LückingC B, DürrA, BonifatiV, VaughanJ, De MicheleG, GasserT, HarhangiB S, MecoG, DenèfleP, WoodN W, AgidY, BriceA, and the French Parkinson’s Disease Genetics Study Group, and the European Consortium on Genetic Susceptibility in Parkinson’s Disease (2000). Association between early-onset Parkinson’s disease and mutations in the parkin gene. N Engl J Med, 342(21): 1560–1567 doi: 10.1056/NEJM200005253422103 pmid: 10824074
88	LuoL, HenschT K, AckermanL, BarbelS, JanL Y, JanY N (1996). Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature, 379(6568): 837–840 doi: 10.1038/379837a0 pmid: 8587609
89	MaciverS K, HarringtonC R (1995). Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies. Neuroreport, 6(15): 1985–1988 doi: 10.1097/00001756-199510010-00008 pmid: 8580423
90	MahammadS, MurthyS N, DidonnaA, GrinB, IsraeliE, PerrotR, BomontP, JulienJ P, KuczmarskiE, OpalP, GoldmanR D (2013). Giant axonal neuropathy-associated gigaxonin mutations impair intermediate filament protein degradation. J Clin Invest, 123(5): 1964–1975 doi: 10.1172/JCI66387 pmid: 23585478
91	ManettoV, SternbergerN H, PerryG, SternbergerL A, GambettiP (1988). Phosphorylation of neurofilaments is altered in amyotrophic lateral sclerosis. J Neuropathol Exp Neurol, 47(6): 642–653 doi: 10.1097/00005072-198811000-00007 pmid: 2459315
92	ManserE, LeungT, SalihuddinH, ZhaoZ S, LimL (1994). A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature, 367(6458): 40–46 doi: 10.1038/367040a0 pmid: 8107774
93	MatusA (1988). Microtubule-associated proteins: their potential role in determining neuronal morphology. Annu Rev Neurosci, 11(1): 29–44 doi: 10.1146/annurev.ne.11.030188.000333 pmid: 3284444
94	MinamideL S, StrieglA M, BoyleJ A, MebergP J, BamburgJ R (2000). Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol, 2(9): 628–636 doi: 10.1038/35023579 pmid: 10980704
95	MitchisonT J, CramerL P (1996). Actin-based cell motility and cell locomotion. Cell, 84(3): 371–379 doi: 10.1016/S0092-8674(00)81281-7 pmid: 8608590
96	MockrinS C, KornE D (1980). Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry, 19(23): 5359–5362 doi: 10.1021/bi00564a033 pmid: 6893804
97	MorfiniG, PiginoG, MizunoN, KikkawaM, BradyS T (2007). Tau binding to microtubules does not directly affect microtubule-based vesicle motility. J Neurosci Res, 85(12): 2620–2630 doi: 10.1002/jnr.21154 pmid: 17265463
98	MoriwakiA, LuY F, TomizawaK, MatsuiH (1998). An immunosuppressant, FK506, protects against neuronal dysfunction and death but has no effect on electrographic and behavioral activities induced by systemic kainate. Neuroscience, 86(3): 855–865 doi: 10.1016/S0306-4522(98)00071-2 pmid: 9692722
99	MorrisonB M, ShuI W, WilcoxA L, GordonJ W, MorrisonJ H (2000). Early and selective pathology of light chain neurofilament in the spinal cord and sciatic nerve of G86R mutant superoxide dismutase transgenic mice. Exp Neurol, 165(2): 207–220 doi: 10.1006/exnr.2000.7457 pmid: 10993681
100	MunozD G, GreeneC, PerlD P, SelkoeD J (1988). Accumulation of phosphorylated neurofilaments in anterior horn motoneurons of amyotrophic lateral sclerosis patients. J Neuropathol Exp Neurol, 47(1): 9–18 doi: 10.1097/00005072-198801000-00002 pmid: 3334727
101	Niebroj-DoboszI, DziewulskaD, JanikP (2006). Auto-antibodies against proteins of spinal cord cells in cerebrospinal fluid of patients with amyotrophic lateral sclerosis (ALS).Folia neuropathologica / Association of Polish Neuropathologists and Medical Research Centre. Polish Academy of Sciences, 44: 191–196
102	NishidaE, IidaK, YonezawaN, KoyasuS, YaharaI, SakaiH (1987). Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA, 84(15): 5262–5266 doi: 10.1073/pnas.84.15.5262 pmid: 3474653
103	NiwaR, Nagata-OhashiK, TakeichiM, MizunoK, UemuraT (2002). Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell, 108(2): 233–246 doi: 10.1016/S0092-8674(01)00638-9 pmid: 11832213
104	OkamotoK, NagaiT, MiyawakiA, HayashiY (2004). Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat Neurosci, 7(10): 1104–1112 doi: 10.1038/nn1311 pmid: 15361876
105	OuyangY, YangX F, HuX Y, Erbayat-AltayE, ZengL H, LeeJ M, WongM (2007). Hippocampal seizures cause depolymerization of filamentous actin in neurons independent of acute morphological changes. Brain Res, 1143: 238–246 doi: 10.1016/j.brainres.2007.01.077 pmid: 17320053
106	PatrickG N, ZukerbergL, NikolicM, de la MonteS, DikkesP, TsaiL H (1999). Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature, 402(6762): 615–622 doi: 10.1038/45159 pmid: 10604467
107	PavlikL L, MoshkovD A (1991). Actin in synaptic cytoskeleton during long-term potentiation in hippocampal slices. Acta Histochem Suppl, 41(Supp 41): 257–264 pmid: 1811261
108	Pérez-OlléR, López-ToledanoM A, GoryunovD, Cabrera-PochN, StefanisL, BrownK, LiemR K (2005). Mutations in the neurofilament light gene linked to Charcot-Marie-Tooth disease cause defects in transport. J Neurochem, 93(4): 861–874 doi: 10.1111/j.1471-4159.2005.03095.x pmid: 15857389
109	PerrotR, BergesR, BocquetA, EyerJ (2008). Review of the multiple aspects of neurofilament functions, and their possible contribution to neurodegeneration. Mol Neurobiol, 38(1): 27–65 doi: 10.1007/s12035-008-8033-0 pmid: 18649148
110	PowellK J, HoriS E, LeslieR, AndrieuxA, SchellinckH, ThorneM, RobertsonG S (2007). Cognitive impairments in the STOP null mouse model of schizophrenia. Behav Neurosci, 121(5): 826–835 doi: 10.1037/0735-7044.121.5.826 pmid: 17907815
111	PrineasJ W, OuvrierR A, WrightR G, WalshJ C, McLeodJ G (1976). Gian axonal neuropathy—a generalized disorder of cytoplasmic microfilament formation. J Neuropathol Exp Neurol, 35(4): 458–470 doi: 10.1097/00005072-197607000-00006 pmid: 180266
112	QiangL, YuW, AndreadisA, LuoM, BaasP W (2006). Tau protects microtubules in the axon from severing by katanin. J Neurosci, 26(12): 3120–3129 doi: 10.1523/JNEUROSCI.5392-05.2006 pmid: 16554463
113	RaoM V, MohanP S, KumarA, YuanA, MontagnaL, CampbellJ, Veeranna, EspreaficoE M, JulienJ P, NixonR A (2011). The myosin Va head domain binds to the neurofilament-L rod and modulates endoplasmic reticulum (ER) content and distribution within axons. PLoS ONE, 6(2): e17087 doi: 10.1371/journal.pone.0017087 pmid: 21359212
114	RenY, JiangH, YangF, NakasoK, FengJ (2009). Parkin protects dopaminergic neurons against microtubule-depolymerizing toxins by attenuating microtubule-associated protein kinase activation. J Biol Chem, 284(6): 4009–4017 doi: 10.1074/jbc.M806245200 pmid: 19074146
115	RenY, ZhaoJ, FengJ (2003). Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J Neurosci, 23(8): 3316–3324 pmid: 12716939
116	RexC S, ChenL Y, SharmaA, LiuJ, BabayanA H, GallC M, LynchG (2009). Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation. J Cell Biol, 186(1): 85–97 doi: 10.1083/jcb.200901084 pmid: 19596849
117	RossiterJ P, AndersonL L, YangF, ColeG M (2000). Caspase-cleaved actin (fractin) immunolabelling of Hirano bodies. Neuropathol Appl Neurobiol, 26(4): 342–346 doi: 10.1046/j.1365-2990.2000.00252.x pmid: 10931367
118	RossollW, JablonkaS, AndreassiC, KröningA K, KarleK, MonaniU R, SendtnerM (2003). Smn, the spinal muscular atrophy-determining gene product, modulates axon growth and localization of beta-actin mRNA in growth cones of motoneurons. J Cell Biol, 163(4): 801–812 doi: 10.1083/jcb.200304128 pmid: 14623865
119	Rovelet-LecruxA, CampionD (2012). Copy number variations involving the microtubule-associated protein tau in human diseases. Biochem Soc Trans, 40(4): 672–676 doi: 10.1042/BST20120045 pmid: 22817714
120	RoyS, ZhangB, LeeV M, TrojanowskiJ Q (2005). Axonal transport defects: a common theme in neurodegenerative diseases. Acta Neuropathol, 109(1): 5–13 doi: 10.1007/s00401-004-0952-x pmid: 15645263
121	RubioM D, HaroutunianV, Meador-WoodruffJ H (2012). Abnormalities of the Duo/Ras-related C3 botulinum toxin substrate 1/p21-activated kinase 1 pathway drive myosin light chain phosphorylation in frontal cortex in schizophrenia. Biol Psychiatry, 71(10): 906–914 doi: 10.1016/j.biopsych.2012.02.006 pmid: 22458949
122	SánchezC, ArellanoJ I, Rodríguez-SánchezP, AvilaJ, DeFelipeJ, Díez-GuerraF J (2001). Microtubule-associated protein 2 phosphorylation is decreased in the human epileptic temporal lobe cortex. Neuroscience, 107(1): 25–33 doi: 10.1016/S0306-4522(01)00338-4 pmid: 11744243
123	SánchezC, Díaz-NidoJ, AvilaJ (2000). Phosphorylation of microtubule-associated protein 2 (MAP2) and its relevance for the regulation of the neuronal cytoskeleton function. Prog Neurobiol, 61(2): 133–168 doi: 10.1016/S0301-0082(99)00046-5 pmid: 10704996
124	ScheibelM E, CrandallP H, ScheibelA B (1974). The hippocampal-dentate complex in temporal lobe epilepsy. A Golgi study. Epilepsia, 15(1): 55–80 doi: 10.1111/j.1528-1157.1974.tb03997.x pmid: 4523024
125	SchevzovG, CurthoysN M, GunningP W, FathT (2012). Functional diversity of actin cytoskeleton in neurons and its regulation by tropomyosin. Int Rev Cell Mol Biol, 298: 33–94 doi: 10.1016/B978-0-12-394309-5.00002-X pmid: 22878104
126	SchmidtM L, LeeV M, TrojanowskiJ Q (1989). Analysis of epitopes shared by Hirano bodies and neurofilament proteins in normal and Alzheimer’s disease hippocampus. Lab Invest, 60(4): 513–522 pmid: 2468822
127	SchneiderA B J, BiernatJ, von BergenM, MandelkowE M, MandelkowE M (1999). Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry, 38(12): 3549–3558 doi: 10.1021/bi981874p pmid: 10090741
128	ScottW K, NanceM A, WattsR L, HubbleJ P, KollerW C, LyonsK, PahwaR, SternM B, ColcherA, HinerB C, JankovicJ, OndoW G, AllenF H Jr, GoetzC G, SmallG W, MastermanD, MastagliaF, LaingN G, StajichJ M, SlotterbeckB, BoozeM W, RibbleR C, RampersaudE, WestS G, GibsonR A, MiddletonL T, RosesA D, HainesJ L, ScottB L, VanceJ M, Pericak-VanceM A (2001). Complete genomic screen in Parkinson disease: evidence for multiple genes. JAMA, 286(18): 2239–2244 doi: 10.1001/jama.286.18.2239 pmid: 11710888
129	SeitzA, KojimaH, OiwaK, MandelkowE M, SongY H, MandelkowE (2002). Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J, 21(18): 4896–4905 doi: 10.1093/emboj/cdf503 pmid: 12234929
130	ShimizuH, IwayamaY, YamadaK, ToyotaT, MinabeY, NakamuraK, NakajimaM, HattoriE, MoriN, OsumiN, YoshikawaT (2006). Genetic and expression analyses of the STOP (MAP6) gene in schizophrenia. Schizophr Res, 84(2–3): 244–252 doi: 10.1016/j.schres.2006.03.017 pmid: 16624526
131	SousaV L, BellaniS, GiannandreaM, YousufM, ValtortaF, MeldolesiJ, ChieregattiE (2009). alpha-synuclein and its A30P mutant affect actin cytoskeletal structure and dynamics. Mol Biol Cell, 20(16): 3725–3739 doi: 10.1091/mbc.E08-03-0302 pmid: 19553474
132	SternbergerL A, SternbergerN H (1983). Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ. Proc Natl Acad Sci USA, 80(19): 6126–6130 doi: 10.1073/pnas.80.19.6126 pmid: 6577472
133	SudoH, BaasP W (2011). Strategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases. Hum Mol Genet, 20(4): 763–778 doi: 10.1093/hmg/ddq521 pmid: 21118899
134	SweetR A, HenteleffR A, ZhangW, SampsonA R, LewisD A (2009). Reduced dendritic spine density in auditory cortex of subjects with schizophrenia. Neuropsychopharmacology, 34(2): 374–389 doi: 10.1038/npp.2008.67 pmid: 18463626
135	TakeuchiH, KobayashiY, YoshiharaT, NiwaJ, DoyuM, OhtsukaK, SobueG (2002). Hsp70 and Hsp40 improve neurite outgrowth and suppress intracytoplasmic aggregate formation in cultured neuronal cells expressing mutant SOD1. Brain Res, 949(1–2): 11–22 doi: 10.1016/S0006-8993(02)02568-4 pmid: 12213295
136	TilocaC, TicozziN, PensatoV, CorradoL, Del BoR, BertolinC, FenoglioC, GagliardiS, CaliniD, LauriaG, CastellottiB, BagarottiA, CortiS, GalimbertiD, CagninA, GabelliC, RanieriM, CeroniM, SicilianoG, MazziniL, CeredaC, ScarpiniE, SoraruG, ComiGP, D'AlfonsoS, GelleraC, RattiA, LandersJE, SilaniV (2013). Screening of the PFN1 gene in sporadic amyotrophic lateral sclerosis and in frontotemporal dementia. Neurobiol Aging, 34:1517 e1519–1510
137	Torres-BenitoL, RuizR, TabaresL (2012). Synaptic defects in spinal muscular atrophy animal models. Dev Neurobiol, 72(1): 126–133 doi: 10.1002/dneu.20912 pmid: 21567981
138	TortelliR, RuggieriM, CorteseR, D’ErricoE, CapozzoR, LeoA, MastrapasquaM, ZoccolellaS, LeanteR, LivreaP, LogroscinoG, SimoneI L (2012). Elevated cerebrospinal fluid neurofilament light levels in patients with amyotrophic lateral sclerosis: a possible marker of disease severity and progression. Eur J Neurol, 19(12): 1561–1567 doi: 10.1111/j.1468-1331.2012.03777.x pmid: 22680408
139	TrojanowskiJ Q, LeeV M Y (2005). Rous-Whipple Award Lecture. The Alzheimer’s brain: finding out what’s broken tells us how to fix it. Am J Pathol, 167(5): 1183–1188 doi: 10.1016/S0002-9440(10)61206-0 pmid: 16251403
140	TsengY, AnK M, EsueO, WirtzD (2004). The bimodal role of filamin in controlling the architecture and mechanics of F-actin networks. J Biol Chem, 279(3): 1819–1826 doi: 10.1074/jbc.M306090200 pmid: 14594947
141	van BlitterswijkM, BakerMC, BieniekKF, KnopmanDS, JosephsKA, BoeveB, CaselliR, WszolekZK, PetersenR, Graff-RadfordNR, BoylanKB, DicksonDW, RademakersR (2013). Profilin-1 mutations are rare in patients with amyotrophic lateral sclerosis and frontotemporal dementia. Amyotroph Lateral Scler Frontotemporal Degener14:463–469
142	WagnerU, UttonM, GalloJ M, MillerC C (1996). Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation. J Cell Sci, 109(Pt 6): 1537–1543 pmid: 8799840
143	WongN K, HeB P, StrongM J (2000). Characterization of neuronal intermediate filament protein expression in cervical spinal motor neurons in sporadic amyotrophic lateral sclerosis (ALS). J Neuropathol Exp Neurol, 59(11): 972–982 pmid: 11089575
144	WuC H, FalliniC, TicozziN, KeagleP J, SappP C, PiotrowskaK, LoweP, KoppersM, McKenna-YasekD, BaronD M, KostJ E, Gonzalez-PerezP, FoxA D, AdamsJ, TaroniF, TilocaC, LeclercA L, ChafeS C, MangrooD, MooreM J, ZitzewitzJ A, XuZ S, van den BergL H, GlassJ D, SicilianoG, CirulliE T, GoldsteinD B, SalachasF, MeiningerV, RossollW, RattiA, GelleraC, BoscoD A, BassellG J, SilaniV, DroryV E, BrownR H Jr, LandersJ E (2012). Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis. Nature, 488(7412): 499–503 doi: 10.1038/nature11280 pmid: 22801503
145	XieZ, SrivastavaD P, PhotowalaH, KaiL, CahillM E, WoolfreyK M, ShumC Y, SurmeierD J, PenzesP (2007). Kalirin-7 controls activity-dependent structural and functional plasticity of dendritic spines. Neuron, 56(4): 640–656 doi: 10.1016/j.neuron.2007.10.005 pmid: 18031682
146	XuZ, CorkL C, GriffinJ W, ClevelandD W (1993). Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell, 73(1): 23–33 doi: 10.1016/0092-8674(93)90157-L pmid: 8462100
147	YangF, JiangQ, ZhaoJ, RenY, SuttonM D, FengJ (2005). Parkin stabilizes microtubules through strong binding mediated by three independent domains. J Biol Chem, 280(17): 17154–17162 doi: 10.1074/jbc.M500843200 pmid: 15737990
148	YangN, HiguchiO, OhashiK, NagataK, WadaA, KangawaK, NishidaE, MizunoK (1998). Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature, 393(6687): 809–812 doi: 10.1038/31735 pmid: 9655398
149	YangS, FifitaJ A, WilliamsK L, WarraichST, PamphlettR, NicholsonG A, BlairI P (2013). Mutation analysis and immunopathological studies of PFN1 in familial and sporadic amyotrophic lateral sclerosis. Neurobiol Aging, 34:2235 e2237–2210
150	YoshiharaT, YamamotoM, HattoriN, MisuK, MoriK, KoikeH, SobueG (2002). Identification of novel sequence variants in the neurofilament-light gene in a Japanese population: analysis of Charcot-Marie-Tooth disease patients and normal individuals. J Peripher Nerv Syst, 7(4): 221–224 doi: 10.1046/j.1529-8027.2002.02028.x pmid: 12477167
151	ZengL H, XuL, RensingN R, SinatraP M, RothmanS M, WongM (2007). Kainate seizures cause acute dendritic injury and actin depolymerization in vivo. J Neurosci, 27(43): 11604–11613 doi: 10.1523/JNEUROSCI.0983-07.2007 pmid: 17959803
152	ZhangB, CarrollJ, TrojanowskiJ Q, YaoY, IbaM, PotuzakJ S, HoganA M L, XieS X, BallatoreC, SmithA B 3rd, LeeV M L, BrundenK R (2012). The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J Neurosci, 32(11): 3601–3611 doi: 10.1523/JNEUROSCI.4922-11.2012 pmid: 22423084
153	ZhangB, MaitiA, ShivelyS, LakhaniF, McDonald-JonesG, BruceJ, LeeE B, XieS X, JoyceS, LiC, ToleikisP M, LeeV M, TrojanowskiJ Q (2005). Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model. Proc Natl Acad Sci USA, 102(1): 227–231 doi: 10.1073/pnas.0406361102 pmid: 15615853
154	ZhangW, BensonD L (2001). Stages of synapse development defined by dependence on F-actin. J Neurosci,21:5169–5181
155	ZhuQ, Couillard-DesprésS, JulienJ P (1997). Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments. Exp Neurol, 148(1): 299–316 doi: 10.1006/exnr.1997.6654 pmid: 9398473
156	ZouZY, SunQ, LiuMS, LiXG, CuiLY (2013). Mutations in the profilin 1 gene are not common in amyotrophic lateral sclerosis of Chinese origin. Neurobiol Aging, 34:1713 e1715–1716

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