Function
Tyrosine phosphatase or Protein tyrosine phosphatase (PTP) is an enzyme which removes phosphate from phosphorylated tyrosine residues. It is a key regulatory component of signal transduction pathways[1]. PTPs are divided to 4 subfamilies.
- PTP class I contains receptor PTPs (RPTP) and dual-specificity PTP which removes phosphate from Ser/Thr and tyrosine. Human PTP PRL is found in regenerating liver.
- PTP class II are low molecular weight PTP which dephosphorylate a number of growth factors and modulate their signalling processes[2].
- PTP class III contains CDC25 which removes phosphate from Thr and tyrosine. PTP containing SH2 domains are called PTP SHP.
- Non-receptor type PTPs are coded by the PTPN genes.
For details of PTP complex with inhibitor see Student Projects for UMass Chemistry 423 Spring 2012-9.
Disease
PTP mutations are involved in cancers[3].
3D Structures of tyrosine phosphatase
Tyrosine phosphatase 3D structures
References
- ↑ Paul S, Lombroso PJ. Receptor and nonreceptor protein tyrosine phosphatases in the nervous system. Cell Mol Life Sci. 2003 Nov;60(11):2465-82. PMID:14625689 doi:http://dx.doi.org/10.1007/s00018-003-3123-7
- ↑ Caselli A, Paoli P, Santi A, Mugnaioni C, Toti A, Camici G, Cirri P. Low molecular weight protein tyrosine phosphatase: Multifaceted functions of an evolutionarily conserved enzyme. Biochim Biophys Acta. 2016 Oct;1864(10):1339-55. doi:, 10.1016/j.bbapap.2016.07.001. Epub 2016 Jul 13. PMID:27421795 doi:http://dx.doi.org/10.1016/j.bbapap.2016.07.001
- ↑ Ostman A, Hellberg C, Bohmer FD. Protein-tyrosine phosphatases and cancer. Nat Rev Cancer. 2006 Apr;6(4):307-20. PMID:16557282 doi:http://dx.doi.org/10.1038/nrc1837
