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Synhibin: A new calcium-dependent membrane-binding protein that inhibits synexin-induced chromaffin granule aggregation and fusion
- Source :
- FEBS Letters. (1):201-206
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- We report the isolation and purification of synhibin, a new M r 68000 protein, which inhibits synexin. Synexin mediates Ca 2+ -dependent chromaffin granule aggregation and fusion, processes perhaps important during exocytosis. Our data indicate that synhibin action involves competition with synexin for a site on the chromaffin granule membrane involved in membrane contact. Synhibin may thus be an important intracellular regulator of synexin action during secretion.
- Subjects :
- endocrine system
Biophysics
Regulator
chemistry.chemical_element
Calcium
Biochemistry
Exocytosis
Structural Biology
Genetics
Animals
Secretion
Annexin A7
Chromaffin Granules
Chromaffin granule
Fusion
Molecular Biology
Synhibin
Calcium-Binding Proteins
Membrane aggregation
Membrane Proteins
Proteins
Cell Biology
Chromaffin granule membrane
Chromatography, Ion Exchange
Cell biology
A-site
Kinetics
Membrane
chemistry
Chromaffin System
Synexin
Cattle
Electrophoresis, Polyacrylamide Gel
Carrier Proteins
Intracellular
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....15859739cf6b080ca9a82589f782b8c2
- Full Text :
- https://doi.org/10.1016/0014-5793(82)81334-3