PI(4,5)P₂-dependent regulation of exocytosis by amisyn, the vertebrate-specific competitor of synaptobrevin 2.

ABSTRACT: The functions of nervous and neuroendocrine systems rely on fast and tightly regulated release of neurotransmitters stored in secretory vesicles through SNARE-mediated exocytosis. Few proteins, including tomosyn (STXBP5) and amisyn (STXBP6), were proposed to negatively regulate exocytosis. Little is known about amisyn, a 24-kDa brain-enriched protein with a SNARE motif. We report here that full-length amisyn forms a stable SNARE complex with syntaxin-1 and SNAP-25 through its C-terminal SNARE motif and competes with synaptobrevin-2/VAMP2 for the SNARE-complex assembly. Furthermore, amisyn contains an N-terminal pleckstrin homology domain that mediates its transient association with the plasma membrane of neurosecretory cells by binding to phospholipid PI(4,5)P₂ However, unlike s

SUBMITTER: Kondratiuk I 

PROVIDER: S-EPMC7306819 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature