Involvement of a 65 kDa phosphoprotein in the regulation of membrane fusion during exocytosis inParameciumcells
- 19 October 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 223 (1) , 25-32
- https://doi.org/10.1016/0014-5793(87)80503-3
Abstract
Antisera were raised against a phosphoprotein of 65 kDa (PP65) from Paramecium cells (shown before to be selectively dephosphorylated during synchronous exocytosis) and specified by immunoblotting. By immunofluorescence PP65 has been localized within the cortex, beneath the cell membrane. This corresponds to data obtained by cell fractionation, applying SDS-PAGE autoradiography to cortices prepared from 32P-prelabeled cells. Antisera against PP65 inhibit exocytosis in vivo (microinjection). Applying anti-PP65 antisera in vitro to cortices we could demonstrate inhibition not only of exocytosis, but also of PP65 dephosphorylation. We conclude that PP65 is involved in the regulation of membrane fusion during exocytosis.Keywords
This publication has 38 references indexed in Scilit:
- Membrane capacity, measurements suggest a calcium‐dependent insertion of synexin into phosphatidylserine bilayersFEBS Letters, 1987
- Plenary lecture Mechanism of signal transduction in mast cells and basophils: Studies with RBL-2H3 cellsInflammation Research, 1987
- Calcium-binding proteins and secretionCell Calcium, 1986
- Calmodulin in Paramecium tetraurelia: localization from the in vivo to the ultrastructural level.Journal of Histochemistry & Cytochemistry, 1986
- Filamentous actin in Paramecium cells: mapping by phalloidin affinity labeling in vivo and in vitro.Journal of Histochemistry & Cytochemistry, 1986
- Synchronous exocytosis in Paramecium cells involves very rapid (less than or equal to 1 s), reversible dephosphorylation of a 65-kD phosphoprotein in exocytosis-competent strains.The Journal of cell biology, 1985
- Subcellular location of stimulus-affected endogenous phosphoproteins in the rat parotid gland.The Journal of cell biology, 1984
- Mechanisms of secretion from adrenal chromaffin cellsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1984
- Calcinueurin is a calcium ion-dependent, calmodulin-stimulated protein phosphataseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979