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A pseudosubstrate peptide inhibits protein kinase C‐mediated phosphorylation in permeabilized Rat‐1 cells
Author(s) -
Eichholtz Thomas,
Alblas Jacqueline,
van Overveld Merian,
Moolenaar Wouter,
Ploegh Hidde
Publication year - 1990
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(90)80657-5
Subject(s) - phosphorylation , peptide , microbiology and biotechnology , protein kinase a , chemistry , kinase , biochemistry , biology
Activation of protein kinase C (PKC) in Rat‐1 fibroblasts leads to rapid phosphorylation of an 80‐kDa protein, a major substrate of PKC. Digiton‐in‐permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC 50 of 1 μM, while a control peptide had no effect. The results indicate that this semi‐intact cell system can be used in combination with the inhibitory pseudosubstrate peptide to study the involvement of PKC in cellular processes.