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 invo...
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Published in | FEBS letters Vol. 320; no. 3; pp. 207 - 210 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
12.04.1993
Elsevier |
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Abstract | 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. |
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AbstractList | 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 Ca2+‐dependent secretion and may play a key role in protein‐protein interactions during exocytosis. 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. 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. 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. |
Author | Burgoyne, Robert D. Morgan, Alan Roth, Dagmar |
Author_xml | – sequence: 1 givenname: Dagmar surname: Roth fullname: Roth, Dagmar – sequence: 2 givenname: Alan surname: Morgan fullname: Morgan, Alan – sequence: 3 givenname: Robert D. surname: Burgoyne fullname: Burgoyne, Robert D. |
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Keywords | 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 |
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Snippet | Calcium-dependent secretion in digitonin-permeabilized adrenal chromaffin cells is stimulated by exogenous annexin II and 14-3-3 proteins. These proteins share... Calcium‐dependent secretion in digitonin‐permeabilized adrenal chromaffin cells is stimulated by exogenous annexin II and 14‐3‐3 proteins. These proteins share... |
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SubjectTerms | 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 |
Title | Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells |
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