HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 35, 25089-25096, September 1, 2006

This Article Full Text Full Text (PDF) All Versions of this Article: 281/35/25089    most recent M603591200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mullin, M. J. Articles by Cantrell, D. A. Search for Related Content PubMed PubMed Citation Articles by Mullin, M. J. Articles by Cantrell, D. A. Social Bookmarking                      What's this?

Differential Requirement for RhoA GTPase Depending on the Cellular Localization of Protein Kinase D^*

Michael J. Mullin¹, Kurt Lightfoot¹, Ulrica Marklund², and Doreen A. Cantrell¹³

From the Division of Cell Biology and Immunology, Wellcome Trust Biocentre, University of Dundee, Dundee UK DD1 5EH, Scotland, United Kingdom and the Department of Clinical Immunology, University of Gothenburg, S-413 46 Gothenburg, Sweden

This study explores the links between the GTPase RhoA and the serine kinase protein kinase D (PKD) during thymocyte development. The rationale is that RhoA and PKD regulate common biological responses during T cell development, but there is nothing known about their interdependence. In fibroblasts, Rho function is required for activation of PKD catalytic activity. However, the data show that activation of Rho is neither sufficient nor essential for PKD activation in T cells. One alternative explanation for the apparent convergence of PKD and Rho signaling in T cells is that PKD responses might be Rho-dependent. To address this latter possibility, we probed the Rho requirements for the actions of constitutively active PKD mutants in pre-T cells of transgenic mice. Active PKD can localize to either the plasma membrane or the cytosol, and we therefore compared the Rho requirements for the actions of membrane- or cytosol-localized PKD. Here we show that membrane-localized PKD regulation of pre-T cell differentiation is Rho-dependent, but the actions of cytosol-localized PKD are not. These studies demonstrate that a Rho requirement for PKD activation is not ubiquitous. Moreover, links between PKD and Rho are determined by the cellular location of PKD.

Received for publication, April 13, 2006 , and in revised form, June 12, 2006.

^* This work was supported in part by a program grant from The Wellcome Trust. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by Wellcome Trust Principle Research Fellowship Grant GR065975.

² Supported by European Molecular Biology Organization and Cancer Research, UK.

³ To whom correspondence should be addressed. Tel.: 44-1382-345047; Fax: 44-1382-345783; E-mail: d.a.cantrell{at}dundee.ac.uk.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. F. Cowell, H. Doppler, I. K. Yan, A. Hausser, Y. Umezawa, and P. Storz Mitochondrial diacylglycerol initiates protein-kinase-D1-mediated ROS signaling J. Cell Sci., April 1, 2009; 122(7): 919 - 928. [Abstract] [Full Text] [PDF]