Rabphilin-3A interacts with alpha-actinin, suggesting the Rab3A-rabphilin-3A system regulates actin filament reorganization involved in Ca2+-dependent exocytosis.
May inform models of Ca2+-dependent secretion; leaves open any cardiovascular relevance.
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.
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Kato et al. (1996) studied this question.
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