Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors

被引:61
作者
Mery, L
Magnino, F
Schmidt, K
Krause, KH
Dufour, JF
机构
[1] Univ Bern, Dept Clin Pharmacol, CH-3010 Bern, Switzerland
[2] Univ Hosp Geneva, Div Infect Dis, CH-1211 Geneva 14, Switzerland
[3] Univ Paris 05, Paris, France
[4] Univ Hosp Geneva, Dept Geriatr, CH-1211 Geneva 14, Switzerland
关键词
transient receptor potential protein; inositol 1,4,5-triphosphate receptor; alternative splicing; Ca2+ entry;
D O I
10.1016/S0014-5793(00)02362-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The molecular basis of capacitative (or store-operated) Ca2+ entry is still subject to debate, The transient receptor potential proteins have been hypothesized to be structural components of store-operated Ca2+ channels and recent evidence suggests that Trp3 and its closely related homolog Trp6 are gated by the N-terminal region of the inositol 1,4,5-triphosphate receptors (InsP(3)R). In this study, we report the existence of two isoforms of the human Trp4 protein, referred to as alpha -hTrp4 and beta -hTrp4. The shorter variant beta -hTrp4 is generated through alternative splicing and lacks the C-terminal amino acids G(785)- S-868. Using a yeast two-hybrid assay and glutathione-S-transferase-pulldown experiments, we found that the C-terminus of alpha -hTrp4, but not of beta -hTrp4, associates in vitro with the C-terminal domain of the InsP(3) receptors type 1, 2 and 3. Thus, we describe a novel interaction between Trp proteins and InsP(3)R and me provide evidence suggesting that the formation of hTrp4-InsP(3)R complexes may be regulated by alternative splicing. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:377 / 383
页数:7
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