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 inFEBS letters Vol. 320; no. 3; pp. 207 - 210
Main Authors Roth, Dagmar, Morgan, Alan, Burgoyne, Robert D.
Format Journal Article
LanguageEnglish
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.
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
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Issue 3
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
Language English
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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
URI https://dx.doi.org/10.1016/0014-5793(93)80587-K
https://onlinelibrary.wiley.com/doi/abs/10.1016%2F0014-5793%2893%2980587-K
https://www.ncbi.nlm.nih.gov/pubmed/8462687
https://search.proquest.com/docview/75656760
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