Involvement of a 65 kDa phosphoprotein in the regulation of membrane fusion during exocytosis in Paramecium cells.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Stecher B,Höhne B,Gras U,Momayezi M,Glas-Albrecht R,Plattner H

doi

10.1016/0014-5793(87)80503-3

subject

Has Abstract

pub_date

1987-10-19 00:00:00

pages

25-32

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)80503-3

journal_volume

223

pub_type

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