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Protein & Cell

ISSN 1674-800X

ISSN 1674-8018(Online)

CN 11-5886/Q

Postal Subscription Code 80-984

2018 Impact Factor: 7.575

Prot Cell    2010, Vol. 1 Issue (9) : 802-810    https://doi.org/10.1007/s13238-010-0108-9      PMID: 21203922
REVIEW
Heteromerization of TRP channel subunits: extending functional diversity
Wei Cheng1,2, Changsen Sun1, Jie Zheng2()
1. Lab of Biomedical Optics, College of Physics and Optoelectronic Engineering, Dalian University of Technology, Dalian 116023, China; 2. Department of Physiology and Membrane Biology, University of California School of Medicine, Davis CA 95616, USA
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Abstract

Transient receptor potential (TRP) channels are widely found throughout the animal kingdom. By serving as cellular sensors for a wide spectrum of physical and chemical stimuli, they play crucial physiological roles ranging from sensory transduction to cell cycle modulation. TRP channels are tetrameric protein complexes. While most TRP subunits can form functional homomeric channels, heteromerization of TRP channel subunits of either the same subfamily or different subfamilies has been widely observed. Heteromeric TRP channels exhibit many novel properties compared to their homomeric counterparts, indicating that co-assembly of TRP channel subunits has an important contribution to the diversity of TRP channel functions.

Keywords co-assembly      molecular mechanism      diversification      nonselective cation channel      polymodal receptor      multi-subunit protein complex     
Corresponding Author(s): Zheng Jie,Email:jzheng@ucdavis.edu   
Issue Date: 01 September 2010
 Cite this article:   
Wei Cheng,Changsen Sun,Jie Zheng. Heteromerization of TRP channel subunits: extending functional diversity[J]. Prot Cell, 2010, 1(9): 802-810.
 URL:  
https://academic.hep.com.cn/pac/EN/10.1007/s13238-010-0108-9
https://academic.hep.com.cn/pac/EN/Y2010/V1/I9/802
Fig.1  Topological arrangement of a TRPV channel subunit.
(A) Each channel subunit contains six transmembrane segments (S1-S6), and a pore region formed by a loop between the S5-S6 segments. Long intracellular N and C termini contain several relatively conserved domains such as ankyrin repeat domain (ARD), TRP domain, PDZ domain, CaM binding site. (B) Topological plot of the TRPV ankyrin repeat domain. Red circle represents α-helices, and blue arrows and lines represent β loop fingers.
Fig.1  Topological arrangement of a TRPV channel subunit.
(A) Each channel subunit contains six transmembrane segments (S1-S6), and a pore region formed by a loop between the S5-S6 segments. Long intracellular N and C termini contain several relatively conserved domains such as ankyrin repeat domain (ARD), TRP domain, PDZ domain, CaM binding site. (B) Topological plot of the TRPV ankyrin repeat domain. Red circle represents α-helices, and blue arrows and lines represent β loop fingers.
Fig.2  Subunit association between TRP channel subunits.
(A) Heteromerization of mammalian TRPs. Orange arrows indicate co-assembly between two channel subunits. Purple arrows indicate interaction among three different subunits of the same subfamily. Blue solid arrows indicate interaction between subunits of different subfamilies. Blue dotted arrows indicate functional interaction for which heteromeric channel has not been identified. (B) Co-assembly of TRPs.
Fig.2  Subunit association between TRP channel subunits.
(A) Heteromerization of mammalian TRPs. Orange arrows indicate co-assembly between two channel subunits. Purple arrows indicate interaction among three different subunits of the same subfamily. Blue solid arrows indicate interaction between subunits of different subfamilies. Blue dotted arrows indicate functional interaction for which heteromeric channel has not been identified. (B) Co-assembly of TRPs.
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[1] Haojian Zhang, Shaoguang Li. Molecular mechanisms for survival regulation of chronic myeloid leukemia stem cells[J]. Prot Cell, 2013, 4(3): 186-196.
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