Protein kinase D activation by deletion of its cysteine‐rich motifs

FEBS Letters

Iglesias, Teresa²  Rozengurt, Enrique¹ 

[1] Department of Medicine, UCLA School of Medicine and Molecular Biology Institute, University of California, 900 Veteran Avenue, Warren Hall, Room 11-124, Los Angeles, CA 90095-1786, USA;Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, UK

关键词: Cysteine-rich domain;    Autoinhibition;    Protein kinase C;    Protein kinase D regulation;    CRD;    cysteine-rich domain;    DAG;    diacylglycerol;    PAGE;    polyacrylamide gel electrophoresis;    PDB;    phorbol 12;    13-dibutyrate;    PH;    pleckstrin homology;    PKC;    protein kinase C;    PKD;    protein kinase D;   

DOI  :  10.1016/S0014-5793(99)00772-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protein kinase D is a serine/threonine kinase that binds phorbol esters in a phospholipid-dependent manner via a tandemly repeated cysteine-rich, zinc finger-like motif (the cysteine-rich domain). Here, we examined whether the cysteine-rich domain plays an additional role in the control of the catalytic kinase activity independently of the binding of allosteric effectors. We found that deletion of cys1, cys2 or the entire cysteine-rich domain increases the basal activity of protein kinase D leading to a constitutively active form of this enzyme. Our results demonstrate, for the first time, that the cysteine-rich domain of Protein kinase D plays a negative role in the regulation of protein kinase D kinase activity.

【 授权许可】

Unknown