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Novel phosphorylation site markers of protein kinase C delta activation
Author(s) -
Durgan Joanne,
Michael Nicholas,
Totty Nick,
Parker Peter J.
Publication year - 2007
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/j.febslet.2007.06.035
Subject(s) - autophosphorylation , protein kinase c , phosphorylation , gene isoform , microbiology and biotechnology , kinase , chemistry , protein kinase a , map2k7 , enzyme activator , biology , biochemistry , cyclin dependent kinase 2 , gene
Protein kinase C delta (PKCδ) is a Ser/Thr kinase which regulates numerous cellular processes, including proliferation, differentiation, migration and apoptosis. Here, we demonstrate that PKCδ undergoes in vitro autophosphorylation at three sites within its V3 region (S299, S302, S304), each of which is unique to this PKC isoform and evolutionarily conserved. We demonstrate that S299 and S304 can be phosphorylated in mammalian cells following phorbol ester stimulation and that S299‐phosphorylated PKCδ is localised to both the plasma and nuclear membranes. These data indicate that PKCδ is phosphorylated upon activation and that phospho‐S299 represents a useful marker of the activated enzyme.