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Cyclic AMP‐dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane
Author(s) -
Sarkadi B.,
Enyedi Ágnes,
Faragó Anna,
Mészáros G.,
Kremmer T.,
Gárdos G.
Publication year - 1983
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(83)80378-0
Subject(s) - protein kinase a , microbiology and biotechnology , lymphocyte , membrane , chemistry , biophysics , adenylate kinase , biochemistry , kinase , biology , enzyme , immunology
Inside‐out vesicles from lymphocyte plasma membrane were phosphorylated in the presence of [γ‐ 32 P]ATP. The dissociated catalytic subunit of cyclic AMP‐dependent protein kinase stimulated both membrane protein and membrane lipid phosphorylation, indicating the presence of a phosphorylation cascade. The phosphorylated membrane lipids were analyzed by thin‐layer chromatography. Increase of 32 P‐labelling stimulated by the cyclic AMP‐dependent protein kinase was found exclusively in polyphosphoinositides.