p42 MAPK phosphorylates 80 kDa MARCKS at Ser‐113

FEBS Letters

Schp̈nwaβer, Dorothee C.¹  Herget, Thomas²  Parker, Peter J.¹  Palmer, Ruth H.¹ 

[1] 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: p42MAPKinase;    MARCKS;    Protein kinase C;    Phosphorylation;   

DOI  :  10.1016/0014-5793(96)00991-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the yristoylated lanine-ich -inase ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

【 授权许可】

Unknown