| Literature DB >> 8943213 |
M Kato1, T Sasaki, T Ohya, H Nakanishi, H Nishioka, M Imamura, Y Takai.
Abstract
Rabphilin-3A is a downstream target molecule of Rab3A small GTP-binding protein and implicated in Ca2+-dependent neurotransmitter release. Here we have isolated a rabphilin-3A-interacting molecule from a human brain cDNA library by the yeast two-hybrid method and identified it to be alpha-actinin, known to cross-link actin filaments into a bundle. alpha-Actinin interacts with the N-terminal region of rabphilin-3A, with which GTP-Rab3A interacts, and this interaction stimulates the activity of alpha-actinin to cross-link actin filaments into a bundle. The interaction of rabphilin-3A with alpha-actinin is inhibited by guanosine 5'-(3-O-thio)triphosphate-Rab3A. These results suggest that the Rab3A-rabphilin-3A system regulates the alpha-actinin-regulated reorganization of actin filaments. It has been shown that reorganization of actin filaments is also involved in Ca2+-dependent exocytosis. Therefore, rabphilin-3A may serve as a linker for Rab3A and cytoskeleton.Entities:
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Year: 1996 PMID： 8943213 DOI： 10.1074/jbc.271.50.31775
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157