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VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX

Alonso, A ; Narisawa, S ; Bogetz, J ; Tautz, L ; Hadzic, Radinka LU ; Huynh, H ; Williams, S ; Gjörloff Wingren, Anette LU ; Bremer, MCD and Holsinger, LJ , et al. (2004) In Journal of Biological Chemistry 279(31). p.32586-32591
Abstract
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... (More)
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. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
279
issue
31
pages
32586 - 32591
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • wos:000222849700075
  • scopus:2942552996
ISSN
1083-351X
DOI
10.1074/jbc.M403442200
language
English
LU publication?
yes
additional info
Department affilation moved from v1000588 (Tumour Biology, Malmö) to v1000562 (Department of Translational Medicine) on 2016-01-18 14:39:30.
id
e544f054-c4f1-4301-8602-89ed5538c0ca (old id 271711)
date added to LUP
2016-04-01 12:00:42
date last changed
2025-04-04 14:15:34
@article{e544f054-c4f1-4301-8602-89ed5538c0ca,
  abstract     = {{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.}},
  author       = {{Alonso, A and Narisawa, S and Bogetz, J and Tautz, L and Hadzic, Radinka and Huynh, H and Williams, S and Gjörloff Wingren, Anette and Bremer, MCD and Holsinger, LJ and Millan, JL and Mustelin, T}},
  issn         = {{1083-351X}},
  language     = {{eng}},
  number       = {{31}},
  pages        = {{32586--32591}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX}},
  url          = {{http://dx.doi.org/10.1074/jbc.M403442200}},
  doi          = {{10.1074/jbc.M403442200}},
  volume       = {{279}},
  year         = {{2004}},
}