The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32586-32591
2004
Details
- Autor(en) / Beteiligte
- Titel
- VHY, a Novel Myristoylated Testis-restricted Dual Specificity Protein Phosphatase Related to VHX
- Ist Teil von
- The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32586-32591
- Ort / Verlag
- United States: American Society for Biochemistry and Molecular Biology
- Erscheinungsjahr
- 2004
- Link zum Volltext
- Quelle
- Electronic Journals Library
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0021-9258, 1083-351XeISSN: 1083-351XDOI: 10.1074/jbc.M403442200Titel-ID: cdi_swepub_primary_oai_lup_lub_lu_se_e544f054_c4f1_4301_8602_89ed5538c0ca
- Format
- –
- Schlagworte
- Amino Acid Motifs, Amino Acid Sequence, Animals, Basic Medicine, Binding Sites, Blotting, Northern, Blotting, Southern, Cancer and Oncology, Cancer och onkologi, Cell Line, Cell Line, Tumor, Cell Membrane - metabolism, Clinical Medicine, Cytoplasm - metabolism, DNA, Complementary - metabolism, Dose-Response Relationship, Drug, Dual-Specificity Phosphatases, Embryo, Mammalian - metabolism, Embryo/metabolism, Fibroblasts - metabolism, Glutathione Transferase - metabolism, Glycine - chemistry, Golgi Apparatus - metabolism, Humans, Immunoblotting, Immunohistochemistry, JNK Mitogen-Activated Protein Kinases, Klinisk medicin, Male, MAP Kinase Kinase 4, Medical and Health Sciences, Medicin och hälsovetenskap, Medicinska och farmaceutiska grundvetenskaper, Mice, Mice, Inbred C57BL, Microbiology in the medical area, Microscopy, Confocal, Microscopy, Fluorescence, Mikrobiologi inom det medicinska området, Mitogen-Activated Protein Kinase Kinases - metabolism, Mitogen-Activated Protein Kinase Phosphatases, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Myristic Acids - chemistry, NIH 3T3 Cells, Nitrophenols - chemistry, Organophosphorus Compounds - chemistry, Phosphoprotein Phosphatase/chemistry, Phosphoprotein Phosphatases - chemistry, Phosphoric Monoester Hydrolases - metabolism, Protein Structure, Tertiary, Protein Tyrosine Phosphatases - chemistry, Protein Tyrosine Phosphatases - metabolism, Protein-Tyrosine-Phosphatase/chemistry/metabolism, Repressor Proteins - chemistry, Repressor Proteins - metabolism, Repressor Proteins/chemistry/metabolism, RNA, Messenger - metabolism, Sequence Homology, Amino Acid, Spermatids - metabolism, Testis - metabolism, Transfection, Vaccinia virus - metabolism