Phosphatase Subfamily PTPRK
Phosphatase Classification: Fold CC1:Superfamily CC1: Family PTP: Subfamily PTPRK
PTPRG is a receptor PTP family involved in metazoan neural development and maybe cancer.
Evolution
PTPRK subfamily is vertebrate specific. There are four copies in human.
Domain Structure
PTPRK has dual intracellular catalytic domains. The canonical extracellular domain combination is a MAM domain, Ig domain and multiple FN3 domain.
MAM domain is essential for homophilic cell-cell interaction and helps determine the specificity of these interactions. Truncated PTPRM is properly expressed at the cell surface but fails to promote cell-cell adhesion. Homophilic cell adhesion is fully restored in a chimeric PTPRM molecule containing the MAM domain of PTPRK. However, this chimeric RPTP mu does not interact with either PTPRK or PTPRM [1].
Functions
PTPRK and PTPRM mediates homophilic cell-cell interaction [1, 2].
PTPRK
Putative tumor suppressor [3].
PTPRK regulates CD4+ T cell development through ERK1/2-mediated signaling [4].
References
- Zondag GC, Koningstein GM, Jiang YP, Sap J, Moolenaar WH, and Gebbink MF. Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain. J Biol Chem. 1995 Jun 16;270(24):14247-50. DOI:10.1074/jbc.270.24.14247 |
- Sap J, Jiang YP, Friedlander D, Grumet M, and Schlessinger J. Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding. Mol Cell Biol. 1994 Jan;14(1):1-9. DOI:10.1128/mcb.14.1.1-9.1994 |
- Zhang Y, Siebert R, Matthiesen P, Yang Y, Ha H, and Schlegelberger B. Cytogenetical assignment and physical mapping of the human R-PTP-kappa gene (PTPRK) to the putative tumor suppressor gene region 6q22.2-q22.3. Genomics. 1998 Jul 15;51(2):309-11. DOI:10.1006/geno.1998.5323 |
- Erdenebayar N, Maekawa Y, Nishida J, Kitamura A, and Yasutomo K. Protein-tyrosine phosphatase-kappa regulates CD4+ T cell development through ERK1/2-mediated signaling. Biochem Biophys Res Commun. 2009 Dec 18;390(3):489-93. DOI:10.1016/j.bbrc.2009.09.117 |
