Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells.
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.
Roth
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D
Physiological Laboratory, University of Liverpool, UK.
Morgan
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A
Burgoyne
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RD
D048948:14-3-3 Proteins; D000313:Adrenal Medulla / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins / Q000737:chemistry* / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D002463:Cell Membrane Permeability; D005089:Exocytosis / Q000187:drug effects*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D017302:Annexins; D009419:Nerve Tissue Proteins; D010455:Peptides; D014446:Tyrosine 3-Monooxygenase; D002118:Calcium