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Identification of a key domain in annexin and 14‐3‐3 proteins that stimulate calcium‐dependent exocytosis in permeabilized adrenal chromaffin cells
Author(s) -
Roth Dagmar,
Morgan Alan,
Burgoyne Robert D.
Publication year - 1993
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(93)80587-k
Subject(s) - exocytosis , secretion , annexin a2 , digitonin , annexin , microbiology and biotechnology , biology , c2 domain , chromaffin cell , calcium binding protein , calcium , biochemistry , chemistry , endocrinology , adrenal medulla , cell , enzyme , membrane , catecholamine , organic chemistry
Calcium‐dependent secretion in digitonin‐permeabilized adrenal chromaffin cells is stimulated by exogenous annexin II and 14‐3‐3 proteins. These proteins share a conserved domain that has been suggested to be involved in specific protein‐protein interactions. We examined whether this domain was involved in secretion by using a synthetic peptide (P16) of sequence KGDYQKALLYLCGGDD corresponding to the C‐terminus of annexin II. P16, but not truncated peptides, prevented the stimulation of secretion by 14‐3‐3 proteins and produced a partial inhibition of control secretion. These data suggest that the shared annexin/14‐3‐3 domain is important in the mechanisms controlling Ca 2+ ‐dependent secretion and may play a key role in protein‐protein interactions during exocytosis.