Dissimilar phorbol ester binding properties of the individual cysteine‐rich motifs of protein kinase D

FEBS Letters

Iglesias, Teresa¹  Rozengurt, Enrique²  Matthews, Sharon¹ 

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

关键词: Cysteine-rich domain;    Phorbol ester binding;    Protein kinase C;    Protein kinase D;    CRD;    cysteine-rich domain;    DAG;    diacylglycerol;    DMEM;    Dulbecco's modified Eagle's medium;    GST;    glutathione S-transferase;    PAGE;    polyacrylamide gel electrophoresis;    PBS;    phosphate buffered saline;    PDB;    phorbol 12;    13-dibutyrate;    PH domain;    pleckstrin homology domain;    PKC;    protein kinase C;    PKD;    protein kinase D;    PS;    phosphatidyl-l-serine;   

DOI  :  10.1016/S0014-5793(98)01189-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protein kinase D (PKD) 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, CRD). Here, we examined whether the individual cysteine-rich motifs of the CRD of PKD (referred to as cys1 and cys2) are functionally equivalent in mediating phorbol ester binding both in vivo and in vitro. Our results demonstrate that the cys1 and cys2 motifs of the CRD of PKD are functionally dissimilar, with the cys2 motif responsible for the majority of [³H]phorbol 12,13-dibutyrate (PDB) binding, both in vivo and in vitro.

【 授权许可】

Unknown