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 Lettjournal_title
FEBS lettersauthors
Stecher B,Höhne B,Gras U,Momayezi M,Glas-Albrecht R,Plattner Hdoi
10.1016/0014-5793(87)80503-3subject
Has Abstractpub_date
1987-10-19 00:00:00pages
25-32issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(87)80503-3journal_volume
223pub_type
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