PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

FEBS Letters

Herget, Thomas³  Pappin, Darryl J.C.¹  Parker, Peter J.²  Palmer, Ruth H.²  Rahman, Dinah¹  Schönwaßer, Dorothee C.² 

[1] Protein Sequencing Laboratory, Imperial Cancer Research Fund, PO Box 123, Lincoln's Inn Fields, London, WC2A 3PX, UK;Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, PO Box 123, Lincoln's Inn Fields, London, WC2A 3PX, UK;Institute of Physiological Chemistry, University of Mainz, Mainz, Germany

关键词: Protein kinase C;    PKC;    PRK;    MARCKS;    Phosphorylation;   

DOI  :  10.1016/0014-5793(95)01454-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown