Difference between revisions of "Phosphatase Subfamily PTPN6"
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The PTPN6/SHP subfamiy is under extensive studies and see more in reviews (e.g. <cite>Neel03, Lorenz09</cite>) and papers. | The PTPN6/SHP subfamiy is under extensive studies and see more in reviews (e.g. <cite>Neel03, Lorenz09</cite>) and papers. | ||
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| + | ===== Miscellaneous ===== | ||
| + | PTPN6/SHP-1 dephosphorylates and inhibites Transient receptor potential vanilloid 1 (TRPV1) receptors in rat dorsal root ganglions (DRGs). [http://en.wikipedia.org/wiki/TRPV1 TRPV1] is a nonselective cation channel that provides sensation of scalding heat and pain (nociception). | ||
===References=== | ===References=== | ||
Revision as of 17:24, 26 March 2015
Phosphatase Classification: Fold CC1:Superfamily CC1: Family PTP: Subfamily PTPN6 (SHP)
Evolution
The PTPN6 subfamily is found across holozoa. It is a single copy in most invertebrate genomes and two or three copies in most vertebrates. Human has two members, PTPN6 (SHP1) and PTPN11 (SHP2).
Domain
The PTPN6 subfamily has two tandem SH2 domains and phosphatase domain. Besides the structural domains, it has a C-terminal tail important for the regulation of its function [1].
Functions
Human PTPN6 (SHP-1) and PTPN11 (SHP-2) are proposed to have different roles in signal transduction: PTPN6/SHP-1 plays a largely negative signalling role, whereas PTPN11/SHP-2 plays a largely positive role in cell signalling leading to cell activation. Expression of PTPN6/SHP-1 is restricted mainly to haematopoietic cells whereas PTPN11/SHP-2 is more widely expressed; both enzymes are expressed in many haematopoietic cells [1].
The PTPN6/SHP subfamiy is under extensive studies and see more in reviews (e.g. [2, 3]) and papers.
Miscellaneous
PTPN6/SHP-1 dephosphorylates and inhibites Transient receptor potential vanilloid 1 (TRPV1) receptors in rat dorsal root ganglions (DRGs). TRPV1 is a nonselective cation channel that provides sensation of scalding heat and pain (nociception).
References
- Poole AW and Jones ML. A SHPing tale: perspectives on the regulation of SHP-1 and SHP-2 tyrosine phosphatases by the C-terminal tail. Cell Signal. 2005 Nov;17(11):1323-32. DOI:10.1016/j.cellsig.2005.05.016 |
- Neel BG, Gu H, and Pao L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem Sci. 2003 Jun;28(6):284-93. DOI:10.1016/S0968-0004(03)00091-4 |
- Lorenz U. SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels. Immunol Rev. 2009 Mar;228(1):342-59. DOI:10.1111/j.1600-065X.2008.00760.x |
