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Involvement of a 65 kDa phosphoprotein in the regulation of membrane fusion during exocytosis in Paramecium cells
Author(s) -
Stecher Brigitte,
Höhne Barbara,
Gras Ute,
Momayezi Massoud,
Glas-Albrecht René,
Plattner Helmut
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80503-3
Subject(s) - exocytosis , microbiology and biotechnology , phosphoprotein , paramecium , dephosphorylation , lipid bilayer fusion , ectodomain , cell fractionation , endocytosis , biology , chemistry , secretion , membrane , cell , biochemistry , phosphorylation , receptor , phosphatase
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 32 P‐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.