PTPRR explained

Protein tyrosine phosphatase receptor-type R is an enzyme that in humans is encoded by the PTPRR gene.^{[1] [2] [3]}

Function

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 a single intracellular catalytic domains, and thus represents a receptor-type PTP. The similar gene predominantly expressed in mouse brain was found to associate with, and thus regulate the activity and cellular localization of MAP kinases. The rat counterpart of this gene was reported to be regulated by the nerve growth factor, which suggested the function of this gene in neuronal growth and differentiation.^[3]

Interactions

PTPRR has been shown to interact with MAPK7.^[4]

Further reading

• Sharma E, Lombroso PJ . A neuronal protein tyrosine phosphatase induced by nerve growth factor. . J. Biol. Chem. . 270 . 1 . 49–53 . 1995 . 7814416 . 10.1074/jbc.270.1.49 . free .
• Ogata M, Sawada M, Fujino Y, Hamaoka T . cDNA cloning and characterization of a novel receptor-type protein tyrosine phosphatase expressed predominantly in the brain. . J. Biol. Chem. . 270 . 5 . 2337–43 . 1995 . 7836467 . 10.1074/jbc.270.5.2337 . free .
• Pulido R, Zúñiga A, Ullrich A . PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. . EMBO J. . 17 . 24 . 7337–50 . 1999 . 9857190 . 1171079 . 10.1093/emboj/17.24.7337 .
• Ogata M, Oh-hora M, Kosugi A, Hamaoka T . Inactivation of mitogen-activated protein kinases by a mammalian tyrosine-specific phosphatase, PTPBR7. . Biochem. Biophys. Res. Commun. . 256 . 1 . 52–6 . 1999 . 10066421 . 10.1006/bbrc.1999.0278 .
• Zúñiga A, Torres J, Ubeda J, Pulido R . Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. . J. Biol. Chem. . 274 . 31 . 21900–7 . 1999 . 10419510 . 10.1074/jbc.274.31.21900 . free . 10550/84237 . free .
• Blanco-Aparicio C, Torres J, Pulido R . A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. . J. Cell Biol. . 147 . 6 . 1129–36 . 2000 . 10601328 . 2168101 . 10.1083/jcb.147.6.1129 .
• Augustine KA, Silbiger SM, Bucay N, Ulias L, Boynton A, Trebasky LD, Medlock ES . Protein tyrosine phosphatase (PC12, Br7,S1) family: expression characterization in the adult human and mouse. . Anat. Rec. . 258 . 3 . 221–34 . 2000 . 10705342 . 10.1002/(SICI)1097-0185(20000301)258:3<221::AID-AR1>3.0.CO;2-W . free .
• Bektas A, Hughes JN, Warram JH, Krolewski AS, Doria A . Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes. . Diabetes . 50 . 1 . 204–8 . 2001 . 11147789 . 10.2337/diabetes.50.1.204 . free .
• Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ . Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation. . J. Mol. Biol. . 311 . 3 . 557–68 . 2001 . 11493009 . 10.1006/jmbi.2001.4890 .
• Buschbeck M, Eickhoff J, Sommer MN, Ullrich A . Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway. . J. Biol. Chem. . 277 . 33 . 29503–9 . 2002 . 12042304 . 10.1074/jbc.M202149200 . free .
• Shin BK, Wang H, Yim AM, Le Naour F, Brichory F, Jang JH, Zhao R, Puravs E, Tra J, Michael CW, Misek DE, Hanash SM . Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. . J. Biol. Chem. . 278 . 9 . 7607–16 . 2003 . 12493773 . 10.1074/jbc.M210455200 . free .
• Tárrega C, Ríos P, Cejudo-Marín R, Blanco-Aparicio C, van den Berk L, Schepens J, Hendriks W, Tabernero L, Pulido R . ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1. . J. Biol. Chem. . 280 . 45 . 37885–94 . 2006 . 16148006 . 10.1074/jbc.M504366200 . free . 2066/48764 . free .
• Eswaran J, von Kries JP, Marsden B, Longman E, Debreczeni JE, Ugochukwu E, Turnbull A, Lee WH, Knapp S, Barr AJ . Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases. . Biochem. J. . 395 . 3 . 483–91 . 2006 . 16441242 . 1462698 . 10.1042/BJ20051931 .

Notes and References

1. Shiozuka K, Watanabe Y, Ikeda T, Hashimoto S, Kawashima H . Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase . Gene . 162 . 2 . 279–84 . Nov 1995 . 7557444 . 10.1016/0378-1119(95)00306-Q .
2. van den Maagdenberg AM, Schepens JT, Schepens MT, Merkx GF, Darroudi F, Wieringa B, Geurts van Kessel A, Hendriks WJ . Assignment1 of the PTP-SL/PTPBR7 gene (Ptprr/PTPRR) to mouse chromosome region 8A2 by in situ hybridization . Cytogenet Cell Genet . 84 . 3–4 . 243–4 . Jul 1999 . 10393441 . 10.1159/000015268 . 35964382 .
3. Web site: Entrez Gene: PTPRR protein tyrosine phosphatase, receptor type, R.
4. Buschbeck M, Eickhoff J, Sommer MN, Ullrich A . Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway . J. Biol. Chem. . 277 . 33 . 29503–9 . Aug 2002 . 12042304 . 10.1074/jbc.M202149200 . free .