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

J. Biol. Chem., Vol. 279, Issue 31, 32586-32591, July 30, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/31/32586    most recent M403442200v1 Alert me when this article is cited 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 Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Alonso, A. Articles by Mustelin, T. Search for Related Content PubMed PubMed Citation Articles by Alonso, A. Articles by Mustelin, T. Social Bookmarking                      What's this?

VHY, a Novel Myristoylated Testis-restricted Dual Specificity Protein Phosphatase Related to VHX^*

Andres Alonso, Sonoko Narisawa¶, Jori Bogetz, Lutz Tautz, Radinka Hadzic||, Huong Huynh, Scott Williams, Anette Gjörloff-Wingren||, Meire C. D. Bremer**, Leslie J. Holsinger**, José L. Millan¶, and Tomas Mustelin

From the Program of Signal Transduction and ^¶Program of Stem Cell Biology, Cancer Research Center, The Burnham Institute, La Jolla, California 92037, ^||Department of Medical Microbiology, Lund University, SE-205 02 Malmö, Sweden, and ^**SUGEN Incorporated, South San Francisco, California 94602

The human DUSP15 gene encodes an uncharacterized 235-amino acid member of the subfamily of small dual specificity protein phosphatases related to the Vaccinia virus VH1 phosphatase. Similar to VHR-related MKPX (VHX) (DUSP22), the predicted protein has an N-terminal myristoylation recognition sequence, and we show here that both are indeed modified by the attachment of a myristate to Gly-2. In recognition of this relatedness to VHX, we refer to the DUSP15-encoded protein as VH1-related member Y (VHY). We report that VHY is expressed at high levels in the testis and barely detectable levels in the brain, spinal cord, and thyroid. A VHY-specific antiserum detected a protein with an apparent molecular mass of 26 kDa, and histochemical analysis showed that VHY was readily detectable in pachytene spermatocytes (midstage of meiotic division I) and round spermatids and weakly in Leydig cells (somatic cells outside of the seminiferous tubules). When expressed in 293T or NIH-3T3 cells, VHY was concentrated at the plasma membrane with some staining of vesicular structures in the Golgi region. Mutation of the myristoylation site Gly-2 abrogated membrane location. Finally, we demonstrate that VHY is an active phosphatase in vitro. We conclude that VHY is a new member of a subgroup of myristoylated VH1-like small dual specificity phosphatases.

Received for publication, March 29, 2004 , and in revised form, May 7, 2004.

^* This work was supported by National Institutes of Health Grants AI35603, AI48032, AI53585, AI55741, and CA96949 (to T. M.). 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.

Present address: Universidad de Valladolid, Instituto de Biologia y Genetica Molecular, Facultad de Medicina, c/Ramon y Cajal S/N, 47005 Valladolid, Spain.

To whom correspondence should be addressed: The Burnham Institute, 10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-713-6270; E-mail: tmustelin{at}burnham.org.

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