Premium
Synhibin: A new calcium‐dependent membrane‐binding protein that inhibits synexin‐induced chromaffin granule aggregation and fusion
Author(s) -
Pollard Harvey B.,
Scott Janet H.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81334-3
Subject(s) - exocytosis , granule (geology) , chromaffin cell , lipid bilayer fusion , secretion , chemistry , intracellular , calcium , microbiology and biotechnology , biochemistry , membrane , biology , adrenal medulla , catecholamine , paleontology , organic chemistry , neuroscience
We report the isolation and purification of synhibin, a new M r 68000 protein, which inhibits synexin. Synexin mediates Ca 2+ ‐dependent chromaffin granule aggregation and fusion, processes perhaps important during exocytosis. Our data indicate that synhibin action involves competition with synexin for a site on the chromaffin granule membrane involved in membrane contact. Synhibin may thus be an important intracellular regulator of synexin action during secretion.