Function
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 on Yersinia PTP see Yersinia YopH.
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
