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PTPN12

Introduction

Tyrosine-protein phosphatase non-receptor type 12 is an enzyme that in humans is encoded by the PTPN12 gene.[1][2]

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 contains a C-terminal PEST motif, which serves as a protein–protein interaction domain, and may be related to protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of oncogene c-ABL, thus may play a role in oncogenesis. This PTP was shown to interact with, and dephosphorylate, various of cytoskeleton and cell adhesion molecules, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin, which suggested its regulatory roles in controlling cell shape and mobility.[2]

Interactions

Interactions

PTPN12 has been shown to interact with BCAR1,[3][4][5][6] Grb2,[7] PSTPIP1,[8] TGFB1I1,[9] Paxillin[10][11][12] and SHC1.[13][14]

References

References

  1. ↑ Takekawa M, Itoh F, Hinoda Y, Adachi M, Ariyama T, Inazawa J, Imai K, Yachi A (Mar 1994). “Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells”. FEBS Lett. 339 (3): 222–8. doi:10.1016/0014-5793(94)80420-6. PMID 7509295.
  2. ↑ 2.0 2.1 “Entrez Gene: PTPN12 protein tyrosine phosphatase, non-receptor type 12”.
  3. ↑ Lin, Yi; Ceacareanu Alice Corina; Hassid Aviv (Aug 2003). “Nitric oxide-induced inhibition of aortic smooth muscle cell motility: role of PTP-PEST and adaptor proteins p130cas and Crk”. Am. J. Physiol. Heart Circ. Physiol. United States. 285 (2): H710–21. doi:10.1152/ajpheart.01127.2002. ISSN 0363-6135. PMID 12714323.
  4. ↑ Garton, A J; Burnham M R; Bouton A H; Tonks N K (Aug 1997). “Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition”. Oncogene. ENGLAND. 15 (8): 877–85. doi:10.1038/sj.onc.1201279. ISSN 0950-9232. PMID 9285683.
  5. ↑ Côté, J F; Charest A; Wagner J; Tremblay M L (Sep 1998). “Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model”. Biochemistry. UNITED STATES. 37 (38): 13128–37. doi:10.1021/bi981259l. ISSN 0006-2960. PMID 9748319.
  6. ↑ Garton, A J; Flint A J; Tonks N K (Nov 1996). “Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST”. Mol. Cell. Biol. UNITED STATES. 16 (11): 6408–18. ISSN 0270-7306. PMC 231642. PMID 8887669.
  7. ↑ Charest, A; Wagner J; Kwan M; Tremblay M L (Apr 1997). “Coupling of the murine protein tyrosine phosphatase PEST to the epidermal growth factor (EGF) receptor through a Src homology 3 (SH3) domain-mediated association with Grb2”. Oncogene. ENGLAND. 14 (14): 1643–51. doi:10.1038/sj.onc.1201008. ISSN 0950-9232. PMID 9135065.
  8. ↑ Dowbenko, D; Spencer S; Quan C; Lasky L A (Jan 1998). “Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein”. J. Biol. Chem. UNITED STATES. 273 (2): 989–96. doi:10.1074/jbc.273.2.989. ISSN 0021-9258. PMID 9422760.
  9. ↑ Nishiya, N; Iwabuchi Y; Shibanuma M; Côté J F; Tremblay M L; Nose K (Apr 1999). “Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain”. J. Biol. Chem. UNITED STATES. 274 (14): 9847–53. doi:10.1074/jbc.274.14.9847. ISSN 0021-9258. PMID 10092676.
  10. ↑ Shen, Y; Lyons P; Cooley M; Davidson D; Veillette A; Salgia R; Griffin J D; Schaller M D (Jan 2000). “The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo”. J. Biol. Chem. UNITED STATES. 275 (2): 1405–13. doi:10.1074/jbc.275.2.1405. ISSN 0021-9258. PMID 10625692.
  11. ↑ Côté, J F; Turner C E; Tremblay M L (Jul 1999). “Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST”. J. Biol. Chem. UNITED STATES. 274 (29): 20550–60. doi:10.1074/jbc.274.29.20550. ISSN 0021-9258. PMID 10400685.
  12. ↑ Shen, Y; Schneider G; Cloutier J F; Veillette A; Schaller M D (Mar 1998). “Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin”. J. Biol. Chem. UNITED STATES. 273 (11): 6474–81. doi:10.1074/jbc.273.11.6474. ISSN 0021-9258. PMID 9497381.
  13. ↑ Habib, T; Herrera R; Decker S J (Oct 1994). “Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase”. J. Biol. Chem. UNITED STATES. 269 (41): 25243–6. ISSN 0021-9258. PMID 7929214.
  14. ↑ Charest, A; Wagner J; Jacob S; McGlade C J; Tremblay M L (Apr 1996). “Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity”. J. Biol. Chem. UNITED STATES. 271 (14): 8424–9. doi:10.1074/jbc.271.14.8424. ISSN 0021-9258. PMID 8626541.
Further reading

Further reading