Regular Article
Protein Kinase D Interacts with Golgi via Its Cysteine-Rich Domain

https://doi.org/10.1006/bbrc.2001.5530Get rights and content

Abstract

Protein kinase D (PKD)/protein kinase Cμ is a serine/threonine protein kinase that has been localized in the cytosol and in several intracellular compartments including Golgi, mitochondria and plasma membrane. Using real time imaging of fluorescent protein (GFP)-tagged PKD, we have found that the accumulation of PKD in the Golgi compartment, following a temperature shift from 37 to 20°C, was mediated by the cysteine-rich domain (CRD) of PKD. The CRD of PKD also mediates its interaction with the plasma membrane, further supporting the conclusion that the CRD of PKD may act as a subcellular localization signal.

References (40)

Cited by (28)

  • Diacylglycerol and Protein Kinase D Localization during T Lymphocyte Activation

    2006, Immunity
    Citation Excerpt :

    Accordingly, because PKD-1 can have divergent functions at different intracellular sites, understanding the mechanisms regulating PKD intracellular positioning is fundamental to understanding PKD function in lymphocyte activation. A key determinant for PKD localization is DAG binding to the CRD (Maeda et al., 2001; Rey and Rozengurt, 2001). DAG binding is required for PKD activation in lymphocytes (Wood et al., 2005), but the only information about PKD localization in T cells is that PKD can transiently move to the plasma membrane in T cells activated by CD3 antibodies (Medeiros et al., 2005).

  • Protein kinase D signaling

    2005, Journal of Biological Chemistry
View all citing articles on Scopus
1

The Ronald S. Hirshberg Professor of Translational Pancreatic Cancer Research.

2

To whom correspondence should be addressed at 900 Veteran Avenue, Warren Hall, Room 11-124, Department of Medicine, School of Medicine, University of California at Los Angeles, CA 90095-1786. Fax: (310) 267-2399. E-mail: [email protected].

View full text