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PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163
Author(s) -
Palmer Ruth H.,
Schönwaßer Dorothee C.,
Rahman Dinah,
Pappin Darryl J.C.,
Herget Thomas,
Parker Peter J.
Publication year - 1996
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(95)01454-3
Subject(s) - marcks , protein kinase c , phosphorylation , serine , microbiology and biotechnology , kinase , chemistry , biochemistry , biology
The 80kDa yristolated lanine‐ ich ‐ inase ubstrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid‐activated PKC‐related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.