Difference between revisions of "Phosphatase Subfamily PTPN6"
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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 <cite>Poole05</cite>. | 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 <cite>Poole05</cite>. | ||
| − | 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. Below are some examples of their functions: |
| + | ===== PTPN6 (SHP-1) ===== | ||
PTPN6/SHP-1 dephosphorylates and inhibites Transient receptor potential vanilloid 1 (TRPV1) receptors in rat dorsal root ganglions (DRGs) <cite>Xiao15</cite>. [http://en.wikipedia.org/wiki/TRPV1 TRPV1] is a nonselective cation channel that provides sensation of scalding heat and pain (nociception). | PTPN6/SHP-1 dephosphorylates and inhibites Transient receptor potential vanilloid 1 (TRPV1) receptors in rat dorsal root ganglions (DRGs) <cite>Xiao15</cite>. [http://en.wikipedia.org/wiki/TRPV1 TRPV1] is a nonselective cation channel that provides sensation of scalding heat and pain (nociception). | ||
| + | ===== PTPN11 (SHP-2) ===== | ||
PKA phosphorylates PTPN11/SHP-2 at Thr-73 and Ser-189 in two SH2 domains, respectively. The phosphorylation inhibits ligand-binding mediated by SH2 domains and phosphatase activity <cite>Burmeister15</cite>. | PKA phosphorylates PTPN11/SHP-2 at Thr-73 and Ser-189 in two SH2 domains, respectively. The phosphorylation inhibits ligand-binding mediated by SH2 domains and phosphatase activity <cite>Burmeister15</cite>. | ||
Revision as of 18:52, 17 April 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. Below are some examples of their functions:
PTPN6 (SHP-1)
PTPN6/SHP-1 dephosphorylates and inhibites Transient receptor potential vanilloid 1 (TRPV1) receptors in rat dorsal root ganglions (DRGs) [4]. TRPV1 is a nonselective cation channel that provides sensation of scalding heat and pain (nociception).
PTPN11 (SHP-2)
PKA phosphorylates PTPN11/SHP-2 at Thr-73 and Ser-189 in two SH2 domains, respectively. The phosphorylation inhibits ligand-binding mediated by SH2 domains and phosphatase activity [5].
PTPN11/SHP-2 acts as a regulator of the tyrosyl phosphorylation of FGFR4 and of its immediate target FRS2α, thus being essential for the FGF15/19-mediated activation of the FGFR4/P-ERK1/2/PKC signaling pathway as a integrator of hepatic bile acid and FGF15/FGF19 signaling [6].
References
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