TRPC3: a versatile transducer molecule that serves integration and diversification of cellular signals

被引:12
作者
Groschner, K [1 ]
Rosker, C [1 ]
机构
[1] Karl Franzens Univ Graz, Inst Pharmaceut Sci Pharmacol & Toxicol, A-8010 Graz, Austria
基金
奥地利科学基金会;
关键词
TRPC proteins; Non-selective cation channels; Capacitative Ca2+ stop entry channels; Heteromultimerization; Phospholipase C; Na+ stop; Ca2+ stop exchange; Redox signaling; Lipid rafts;
D O I
10.1007/s00210-005-1054-6
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Transient receptor potential (TRP) proteins have been recognized as sensors for a wide variety of external and internal signals involved in maintenance of cellular homeostasis and control of physiological functions. Evidence of a striking versatility in terms of signal integration and transduction has been reported for members of the canonical (or classical) TRP subfamily (TRPCs). TRPC species are cation channel subunits and emerge as multifunctional signal transduction molecules that are able to function as components of divergent signalplexes. Results obtained in heterologous expression systems suggest TRPC3 as a paradigm of multifunctional signal transduction by a cation channel protein. TRPC3 serves cellular Ca(2+)signaling by multiple mechanisms and may control a variety of distinct physiological functions. In this review, we summarize current knowledge on the properties and possible signaling partners of TRPC3, and discuss the role of TRPC3 channel proteins in cellular signaling networks.
引用
收藏
页码:251 / 256
页数:6
相关论文
共 49 条
[1]   TRPC3-like protein is involved in the capacitative cation entry induced by lα,25-dihydroxy-vitamin D3 in ROS 17/2.8 osteoblastic cells [J].
Baldi, C ;
Vazquez, G ;
Calvo, JC ;
Boland, R .
JOURNAL OF CELLULAR BIOCHEMISTRY, 2003, 90 (01) :197-205
[2]   On the molecular basis and regulation of cellular capacitative calcium entry: Roles for Trp proteins [J].
Birnbaumer, L ;
Zhu, X ;
Jiang, MS ;
Boulay, G ;
Peyton, M ;
Vannier, B ;
Brown, D ;
Platano, D ;
Sadeghi, H ;
Stefani, E ;
Birnbaumer, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (26) :15195-15202
[3]   The TRP ion channel family [J].
Clapham, DE ;
Runnels, LW ;
Strübing, C .
NATURE REVIEWS NEUROSCIENCE, 2001, 2 (06) :387-396
[4]   N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity [J].
Dietrich, A ;
Schnitzler, MMY ;
Emmel, J ;
Kalwa, H ;
Hofmann, T ;
Gudermann, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (48) :47842-47852
[5]  
DIETRICH A, 2005, IN PRESS NAUNYNSCHMI
[6]   Selective association of TRPC channel subunits in rat brain synaptosomes [J].
Goel, M ;
Sinkins, WG ;
Schilling, WP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (50) :48303-48310
[7]   Trp proteins form store-operated cation channels in human vascular endothelial cells [J].
Groschner, K ;
Hingel, S ;
Lintschinger, B ;
Balzer, M ;
Romanin, C ;
Zhu, X ;
Schreibmayer, W .
FEBS LETTERS, 1998, 437 (1-2) :101-106
[8]  
Groschner K, 2004, NOVART FDN SYMP, V258, P263
[9]  
Groschner K, 2004, NOVART FDN SYMP, V258, P231
[10]   Subunit composition of mammalian transient receptor potential channels in living cells [J].
Hofmann, T ;
Schaefer, M ;
Schultz, G ;
Gudermann, T .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (11) :7461-7466