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Protein-protein interaction and functionTRPC channels

Authors
 Kirill Kiselyov  ;  Joo Young Kim  ;  Shmuel Muallem  ;  Weizhong Zeng 
Citation
 PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, Vol.451(1) : 116-124, 2005 
Journal Title
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
ISSN
 0031-6768 
Issue Date
2005
MeSH
Animals ; Calcium/metabolism* ; Calcium Channels/metabolism ; Calcium-Binding Proteins/metabolism ; Calmodulin/metabolism ; Carrier Proteins/metabolism ; Cell Membrane/metabolism ; Endoplasmic Reticulum/metabolism ; Homer Scaffolding Proteins ; Humans ; Inositol 1,4,5-Trisphosphate Receptors ; Membrane Proteins/metabolism ; Mixed Function Oxygenases/metabolism ; Muscle Proteins/metabolism ; Protein Interaction Mapping ; Protein Isoforms/physiology ; Protein Structure, Quaternary ; Receptors, Cytoplasmic and Nuclear/metabolism ; SNARE Proteins/metabolism ; TRPC Cation Channels/physiology* ; Type C Phospholipases/metabolism ; src-Family Kinases/metabolism
Keywords
TRPC channels ; Multimerization ; Scaffolds ; Insertion/retrieval ; ER/PM communication ; Channel gating
Abstract
Since their identification in the concluding years of the last century, the mammalian transient receptor potential (canonical) (TRPC) channels have remained in the limelight as the primary candidates for the Ca2+ entry pathway activated by the hormones, growth factors, and neurotransmitters that exert their effect through activation of PLC. Although TRPC channels have been shown clearly to mediate, at least in part, receptor-activated Ca2+ entry in literally all cell types, several of their central characteristics, as recorded in expression systems using recombinant channels, differ from those of the native receptor-dependent Ca2+ influx channels. The present review attempts to highlight the interaction of TRPC channels with other proteins, which may explain the variability of TRPC channel activation and regulatory mechanisms observed with the native and recombinant channels. These include the homologous and heterotopous interactions of TRPC channel isoforms, the interaction of TRPC channels with calmodulin, PLCγ, IP3 receptors, and with scaffolding proteins like InaD, EBP50/NEHRF, caveolin, Janctate and Homers.
Full Text
http://link.springer.com/article/10.1007%2Fs00424-005-1442-2
DOI
10.1007/s00424-005-1442-2
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers
Yonsei Authors
Kim, Joo Young(김주영) ORCID logo https://orcid.org/0000-0003-2623-1491
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/114733
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