Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells

• Published in: FEBS letters Vol. 320; no. 3; pp. 207 - 210
• Main Authors: Roth, Dagmar, Morgan, Alan, Burgoyne, Robert D.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 12.04.1993; Elsevier
• Subjects: 14-3-3 Protein; 14-3-3 Proteins; 4-(2-hydroxyethyl)-1-piperazineethane sulfonic acid; [ethylenebis(oxyethylenenitrilo)]tetraacetic acid; Adrenal Medulla - metabolism; Amino Acid Sequence; Animals; Annexin; Annexins - chemistry; Annexins - pharmacology; Biological and medical sciences; Calcium - pharmacology; Calcium: Secretion; Cattle; Cell Membrane Permeability; Cell physiology; Chromaffin cell; EGTA; Exocytosis; Exocytosis - drug effects; Fundamental and applied biological sciences. Psychology; HEPES; In Vitro Techniques; Molecular and cellular biology; Molecular Sequence Data; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - pharmacology; Peptides - pharmacology; PKC; protein kinase C; RACK; receptor for activated C-kinase; Secretion. Exocytosis; Structure-Activity Relationship; Tyrosine 3-Monooxygenase; RACK; HEPES; PKC; 14-3-3 Protein; Exocytosis; Chromaffin cell; Calcium: Secretion; Annexin; EGTA; Bovine; Adrenal medulla; Structure function relationship; Mechanism; Binding protein; Vertebrata; Mammalia; Domain structure; Lipocortin; Artiodactyla; Ungulata

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 invo...