PTPRM
Protein tyrosine phosphatase, receptor type, M | |||||||||||||
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File:PBB Protein PTPRM image.jpg PDB rendering based on 1rpm. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | PTPRM ; PTPRL1; R-PTP-MU; RPTPM; RPTPU; hR-PTPu | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 37694 | ||||||||||||
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Species | Human | Mouse | |||||||||||
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RefSeq (mRNA) | n/a | n/a | |||||||||||
RefSeq (protein) | n/a | n/a | |||||||||||
Location (UCSC) | n/a | n/a | |||||||||||
PubMed search | n/a | n/a |
Protein tyrosine phosphatase, receptor type, M, also known as PTPRM, is a human gene.[1]
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion.[1]
References
Further reading
- Gebbink MF, van Etten I, Hateboer G; et al. (1991). "Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase". FEBS Lett. 290 (1–2): 123–30. PMID 1655529.
- Brady-Kalnay SM, Rimm DL, Tonks NK (1995). "Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo". J. Cell Biol. 130 (4): 977–86. PMID 7642713.
- Zondag GC, Koningstein GM, Jiang YP; et al. (1995). "Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain". J. Biol. Chem. 270 (24): 14247–50. PMID 7782276.
- Brady-Kalnay SM, Tonks NK (1994). "Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu". J. Biol. Chem. 269 (45): 28472–7. PMID 7961788.
- Brady-Kalnay SM, Flint AJ, Tonks NK (1993). "Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation". J. Cell Biol. 122 (4): 961–72. PMID 8394372.
- Suijkerbuijk RF, Gebbink MF, Moolenaar WH, Geurts van Kessel A (1993). "Fine mapping of the human receptor-like protein tyrosine phosphatase gene (PTPRM) to 18p11.2 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 64 (3–4): 245–6. PMID 8404049.
- Campan M, Yoshizumi M, Seidah NG; et al. (1996). "Increased proteolytic processing of protein tyrosine phosphatase mu in confluent vascular endothelial cells: the role of PC5, a member of the subtilisin family". Biochemistry. 35 (12): 3797–802. doi:10.1021/bi952552d. PMID 8620001.
- Hoffmann KM, Tonks NK, Barford D (1997). "The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu". J. Biol. Chem. 272 (44): 27505–8. PMID 9346878.
- Brady-Kalnay SM, Mourton T, Nixon JP; et al. (1998). "Dynamic interaction of PTPmu with multiple cadherins in vivo". J. Cell Biol. 141 (1): 287–96. PMID 9531566.
- Serra-Pagès C, Medley QG, Tang M; et al. (1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. PMID 9624153.
- Bianchi C, Sellke FW, Del Vecchio RL; et al. (1999). "Receptor-type protein-tyrosine phosphatase mu is expressed in specific vascular endothelial beds in vivo". Exp. Cell Res. 248 (1): 329–38. doi:10.1006/excr.1999.4428. PMID 10094839.
- Zondag GC, Reynolds AB, Moolenaar WH (2000). "Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn)". J. Biol. Chem. 275 (15): 11264–9. PMID 10753936.
- Blanchetot C, den Hertog J (2000). "Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs". J. Biol. Chem. 275 (17): 12446–52. PMID 10777529.
- Feiken E, van Etten I, Gebbink MF; et al. (2000). "Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity". J. Biol. Chem. 275 (20): 15350–6. PMID 10809770.
- Mourton T, Hellberg CB, Burden-Gulley SM; et al. (2001). "The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts". J. Biol. Chem. 276 (18): 14896–901. doi:10.1074/jbc.M010823200. PMID 11278757.
- Hellberg CB, Burden-Gulley SM, Pietz GE, Brady-Kalnay SM (2002). "Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells". J. Biol. Chem. 277 (13): 11165–73. doi:10.1074/jbc.M112157200. PMID 11801604.
- Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J (2003). "Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases". J. Biol. Chem. 277 (49): 47263–9. doi:10.1074/jbc.M205810200. PMID 12376545.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Koop EA, Lopes SM, Feiken E; et al. (2004). "Receptor protein tyrosine phosphatase mu expression as a marker for endothelial cell heterogeneity; analysis of RPTPmu gene expression using LacZ knock-in mice". Int. J. Dev. Biol. 47 (5): 345–54. PMID 12895029.
- Del Vecchio RL, Tonks NK (2005). "The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase mu". J. Biol. Chem. 280 (2): 1603–12. doi:10.1074/jbc.M410181200. PMID 15491993.
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