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Front Biol    2012, Vol. 7 Issue (5) : 379-396    https://doi.org/10.1007/s11515-012-1244-9
REVIEW
Structure and function of the guanylate kinase-like domain of the MAGUK family scaffold proteins
Jinwei ZHU1, Yuan SHANG1, Jia CHEN1, Mingjie ZHANG1,2()
1. Division of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China; 2. Institute for Advanced Study, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China
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Abstract

Membrane associated guanylate kinases (MAGUKs) are a family of scaffold proteins that play essential roles in organ development, cell-cell communication, cell polarity establishment and maintenance, and cellular signal transduction. Every member of the MAGUK family contains a guanylate kinase-like (GK) domain, which has evolved from the enzyme catalyzing GMP to GDP conversion to become a protein–protein interaction module with no enzymatic activity. Mutations of MAGUKs are linked to a number of human diseases, including autism and hereditary deafness. In this review, we summarize the structural basis governing cellular function of various members of the MAGUKs. In particular, we focus on recent discoveries of MAGUK GKs as specific phospho-protein interaction modules, and discuss functional implications and connections to human diseases of such regulated MAGUK GK/target interactions.
Keywords MAGUK      GK domain      phospho-protein interaction module      synapse      neuronal disease     
Corresponding Author(s): ZHANG Mingjie,Email:mzhang@ust.hk   
Issue Date: 01 October 2012
 Cite this article:   
Jinwei ZHU,Yuan SHANG,Jia CHEN, et al. Structure and function of the guanylate kinase-like domain of the MAGUK family scaffold proteins[J]. Front Biol, 2012, 7(5): 379-396.
 URL:  
https://academic.hep.com.cn/fib/EN/10.1007/s11515-012-1244-9
https://academic.hep.com.cn/fib/EN/Y2012/V7/I5/379
Fig.1  Domain organization of the MAGUK family proteins. All members contain a GK domain with several PDZ domains N and/or C-terminal to the GK domain. All members except for MAGI contain an SH3 domain immediately N-terminal to the GK domain. The CASK and MPP proteins contain a pair of L27 domain connected in tandem in their N-termini. CARMA contains a CARD domain in its N terminus. The Caβs are the smallest and contain only the SH3 and GK domains.
Fig.1  Domain organization of the MAGUK family proteins. All members contain a GK domain with several PDZ domains N and/or C-terminal to the GK domain. All members except for MAGI contain an SH3 domain immediately N-terminal to the GK domain. The CASK and MPP proteins contain a pair of L27 domain connected in tandem in their N-termini. CARMA contains a CARD domain in its N terminus. The Caβs are the smallest and contain only the SH3 and GK domains.
Fig.2  The SH3-GK supramodule. Ribbon diagrams of the PSD-95 SH3-GK tandem (PDB code: 1KJW) (A) and the Caβ SH3-GK tandem (PDB code: 1T3L) (B). The GK domain, the HOOK region and the split SH3 domain are colored green, gray and ruby-red, respectively. The coupling strands between SH3 and GK domain are colored magenta. The N-terminal helix extension in Caβ SH3-GK tandem is colored marine-blue.
Fig.2  The SH3-GK supramodule. Ribbon diagrams of the PSD-95 SH3-GK tandem (PDB code: 1KJW) (A) and the Caβ SH3-GK tandem (PDB code: 1T3L) (B). The GK domain, the HOOK region and the split SH3 domain are colored green, gray and ruby-red, respectively. The coupling strands between SH3 and GK domain are colored magenta. The N-terminal helix extension in Caβ SH3-GK tandem is colored marine-blue.
MAGUKsBinding proteinFunctionReferences
DLG LGNMitotic spindle orientation in ACDZhu et al., 2011
GKAP/DLGAP/SAPAPPostsynaptic scaffold protein; involved in OCDs, ASDsKim et al., 1997; Zhu et al., 2011
SPARRap-specific GTPase-activating proteinPak et al., 2001; Zhu et al., 2011
AKAP79/150Adenylate-kinase anchoring proteinColledge et al., 2000
MAP1aA microtubule-associated proteinBrenman et al., 1998
GAKINKinesin-like motor proteinDeguchi et al., 1998
BEGAINSynaptic scaffold proteinHanada et al., 2000
GukHolderA scaffold protein in synapseMathew et al., 2002
CASKRabphilin3aAn effector of rab3b GTPase; involved in synaptic vesicular traffickingZhang et al., 2001
Tbr-1T-box transcription factorHsueh et al., 2000
CINAPNucleosome assembly protein; together with Tbr-1 involved in regulation of NR2B expressionWang et al., 2004
BCL11A transcriptional repressor; involved in axon outgrowth and branchingKuo et al., 2010
WhirlinA scaffold protein involved in Usher syndromeMburu et al., 2006
MPP1GelsolinActin capping and severing protein; involved in the actin polymerization in hair cell stereociliaMburu et al., 2010
WhirlinA scaffold protein involved in Usher syndromeGosens et al., 2007
MAGIGKAP/DLGAP/SAPAPPostsynaptic scaffold protein; involved in OCDs, ASDsHirao et al., 1998
CavβCavα AID domainModulates gating properties of voltage-gated calcium channelsVan Petegem et al., 2004
Tab.1  Summary of binding partners of MAGUKs GK domains
Fig.3  Structural basis of phosphorylation-dependent target binding of MAGUK GKs. (A) Ribbon diagram representation of the SAP97 SH3-GK/pLGN complex. The SH3 domain is shown in ruby-red, the HOOK region in gray, the Core sub-domain in green, the LID subdomain in orange, and the GMP binding subdomain in blue. The pLGN peptide is shown in purple with the phosphate group shown in the stick-and-ball model. (B) Surface representation showing the GK/pLGN interface. In this drawing, the hydrophobic residues are in yellow, the positively charged residues are in blue, the negatively charged residues are in red, and the rest of the amino acids are in gray. The phospho-LGN peptide, colored in purple, binds to the “Phospho-site” and the “Hydrophobic cradle” in the GMP binding subdomain of SAP97 GK. (C) The amino acid residue conservation map of various GK domains mapped on to the SAP97/pLGN structure. Residues that are conserved (conservation score>0.8) in the DLG subfamily are colored beige; residues that are conserved (conservation score>0.8) among the DLG/MPP/CASK/MAGI subfamilies are colored light blue; other residues are colored light gray. The conservation scores were obtained by the Scorecons Server () based on the amino acid sequence alignment in panel D. (D) Structure-based sequence alignment of the residues of the MAGUK GK GMP binding subdomains. Highly conserved and conserved residues in DLG family are colored red and green, respectively. Residues participating in the phosphate group binding are highlighted in blue-green; residues participating in the hydrophobic cradle binding site are highlighted in orange. (E) Overlay of the GMP binding subdomain of the GK domain structures from MPP1, CASK and DLG1. The GMP binding sites align very well, while the orientations of the core subdomain and LID subdomain vary in different GKs. (F–H) Comparisons of the structures of the yeast guanylate kinase/GMP complex (F), the PSD-95 SH3-GK/GMP complex (G), and the SAP97 SH3-GK/pLGN complex (H).
Fig.3  Structural basis of phosphorylation-dependent target binding of MAGUK GKs. (A) Ribbon diagram representation of the SAP97 SH3-GK/pLGN complex. The SH3 domain is shown in ruby-red, the HOOK region in gray, the Core sub-domain in green, the LID subdomain in orange, and the GMP binding subdomain in blue. The pLGN peptide is shown in purple with the phosphate group shown in the stick-and-ball model. (B) Surface representation showing the GK/pLGN interface. In this drawing, the hydrophobic residues are in yellow, the positively charged residues are in blue, the negatively charged residues are in red, and the rest of the amino acids are in gray. The phospho-LGN peptide, colored in purple, binds to the “Phospho-site” and the “Hydrophobic cradle” in the GMP binding subdomain of SAP97 GK. (C) The amino acid residue conservation map of various GK domains mapped on to the SAP97/pLGN structure. Residues that are conserved (conservation score>0.8) in the DLG subfamily are colored beige; residues that are conserved (conservation score>0.8) among the DLG/MPP/CASK/MAGI subfamilies are colored light blue; other residues are colored light gray. The conservation scores were obtained by the Scorecons Server () based on the amino acid sequence alignment in panel D. (D) Structure-based sequence alignment of the residues of the MAGUK GK GMP binding subdomains. Highly conserved and conserved residues in DLG family are colored red and green, respectively. Residues participating in the phosphate group binding are highlighted in blue-green; residues participating in the hydrophobic cradle binding site are highlighted in orange. (E) Overlay of the GMP binding subdomain of the GK domain structures from MPP1, CASK and DLG1. The GMP binding sites align very well, while the orientations of the core subdomain and LID subdomain vary in different GKs. (F–H) Comparisons of the structures of the yeast guanylate kinase/GMP complex (F), the PSD-95 SH3-GK/GMP complex (G), and the SAP97 SH3-GK/pLGN complex (H).
Fig.4  Structural features of the yeast guanylate kinase and several MAGUK GKs. In all of the drawings, the Core subdomain, GMP binding sub-domain and LID sub-domain are colored green, blue and light-orange, respectively. The corresponding cartoon models are shown below. For clarity, each MAGUK GK is individually compared to the yeast guanylate kinase. (A) The GMP, ATP binding sites in the yeast guanylate kinase. (Left) The apo-form of GK kinase (PDB code: 1EX6); (Right) The ADP- and GMP-bound form of GK kinase (PDB code: 1LVG). (B) DLG GK recognizes phospho-peptides via the GMP binding subdomains. (Left) Comparison of the apo-form of DLG GK (PDB code: 1JXO) with the yeast GK kinase (gray) showing that the GMP binding site is retained and the ATP pocket is blocked in DLG GK. (Right) Structure of the SAP97 SH3-GK/pLGN complex (PDB code: 3UAT). The point mutation (S to P) in the link between the GMP binding subdomain and the Core subdomain marked with a red star in the cartoon below. (C) The Caβ GK domains bind to AID via the ATP binding site. Comparison of the apo-form Caβ GK (PDB code: 1T3S) with the yeast GK kinase (gray) showing that the ATP binding site is enlarged and the GMP binding site is missing in the Caβ GK. (D) The GMP binding site is missing and the ATP binding site is blocked in ZO-subfamily MAGUKs. (Left) Superposition of ZO-1 GK (PDB code: 3SHW) with the yeast GK kinase (gray). The function of this GK domain is unknown.
Fig.4  Structural features of the yeast guanylate kinase and several MAGUK GKs. In all of the drawings, the Core subdomain, GMP binding sub-domain and LID sub-domain are colored green, blue and light-orange, respectively. The corresponding cartoon models are shown below. For clarity, each MAGUK GK is individually compared to the yeast guanylate kinase. (A) The GMP, ATP binding sites in the yeast guanylate kinase. (Left) The apo-form of GK kinase (PDB code: 1EX6); (Right) The ADP- and GMP-bound form of GK kinase (PDB code: 1LVG). (B) DLG GK recognizes phospho-peptides via the GMP binding subdomains. (Left) Comparison of the apo-form of DLG GK (PDB code: 1JXO) with the yeast GK kinase (gray) showing that the GMP binding site is retained and the ATP pocket is blocked in DLG GK. (Right) Structure of the SAP97 SH3-GK/pLGN complex (PDB code: 3UAT). The point mutation (S to P) in the link between the GMP binding subdomain and the Core subdomain marked with a red star in the cartoon below. (C) The Caβ GK domains bind to AID via the ATP binding site. Comparison of the apo-form Caβ GK (PDB code: 1T3S) with the yeast GK kinase (gray) showing that the ATP binding site is enlarged and the GMP binding site is missing in the Caβ GK. (D) The GMP binding site is missing and the ATP binding site is blocked in ZO-subfamily MAGUKs. (Left) Superposition of ZO-1 GK (PDB code: 3SHW) with the yeast GK kinase (gray). The function of this GK domain is unknown.
Fig.5  Possible protein–protein interaction sites in MAGUK SH3-GK tandems illustrated on the structure of the SAP97 SH3-GK supramodule. The GMP binding site colored deep purple; the potential ATP binding site colored red; the canonical SH3 binding pocket colored green; The HOOK region binding site colored blue.
Fig.5  Possible protein–protein interaction sites in MAGUK SH3-GK tandems illustrated on the structure of the SAP97 SH3-GK supramodule. The GMP binding site colored deep purple; the potential ATP binding site colored red; the canonical SH3 binding pocket colored green; The HOOK region binding site colored blue.
Fig.6  Protein complexes related to the spindle orientation in ACD. (A) In , polarized epithelium cells divide symmetrically within the plane of epithelium to expand their pools. (B) neuroblast delaminated from the polarized epithelium undergoes asymmetric cell division to generate a neuroblast and a ganglion mother cell, which divides one more time to give rise to two neurons. (C) A schematic diagram showing several sets of protein complexes that regulate spindle orientations in the neuroblasts.
Fig.6  Protein complexes related to the spindle orientation in ACD. (A) In , polarized epithelium cells divide symmetrically within the plane of epithelium to expand their pools. (B) neuroblast delaminated from the polarized epithelium undergoes asymmetric cell division to generate a neuroblast and a ganglion mother cell, which divides one more time to give rise to two neurons. (C) A schematic diagram showing several sets of protein complexes that regulate spindle orientations in the neuroblasts.
Fig.7  GK domain-mediated protein assemblies in synapses. A schematic diagram showing synaptic signaling complex organization in both pre- and post-synaptic sides of excitatory synapses. For simplicity, only selected sets of synaptic proteins that are directly or indirectly associated with mental disorders are drawn in the figure. The set of proteins labeled in red are known to be high risk factors of ASD.
Fig.7  GK domain-mediated protein assemblies in synapses. A schematic diagram showing synaptic signaling complex organization in both pre- and post-synaptic sides of excitatory synapses. For simplicity, only selected sets of synaptic proteins that are directly or indirectly associated with mental disorders are drawn in the figure. The set of proteins labeled in red are known to be high risk factors of ASD.
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