Historical Background
SAP-1 (also known as PTPRH) was originally identified as a receptor-type protein tyrosine phosphatase (RPTP) expressed in a human stomach cancer cell line (Matozaki et al. 1994). This RPTP belongs to the class II subfamily of RPTPs and is further classified as a member of the R3-subtype of RPTPs, such as DEP-1, VE-PTP, and PTPRO, which are characterized by fibronectin type III-like domains in the extracellular region and a single catalytic domain in the cytoplasmic region (Fig. 1a) (Matozaki et al. 2010). The SAP-1 protein contains eight (human) or six (mouse) fibronectin type III-like domains in its extracellular region (Fig. 1b) (Matozaki et al. 1994; Sadakata et al. 2009). In Drosophila melanogaster, PTP10D, PTP4E, and PTP52F are identified as R3-subtype RPTP family members...
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Chabot C, Spring K, Gratton J-P, Elchebly M, Royal I. New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol Cell Biol. 2009;29:241–53.
Clarke AR. Wnt signalling in the mouse intestine. Oncogene. 2006;25:7512–21.
den Hertog J, Östman A, Böhmer FD. Protein tyrosine phosphatases: regulatory mechanisms. FEBS J. 2008;275:831–47.
Keshavarzian A, Fusunyan RD, Jacyno M, Winship D, MacDermott RP, Sanderson IR. Increased interleukin-8 (IL-8) in rectal dialysate from patients with ulcerative colitis: evidence for a biological role for IL-8 in inflammation of the colon. Am J Gastroenterol. 1999;94:704–12.
Matozaki T, Suzuki T, Uchida T, Inazawa J, Ariyama T, Matsuda K, et al. Molecular cloning of a human transmembrane-type protein tyrosine phosphatase and its expression in gastrointestinal cancers. J Biol Chem. 1994;269:2075–81.
Matozaki T, Murata Y, Mori M, Kotani T, Okazawa H, Ohnishi H. Expression, localization, and biological function of the R3 subtype of receptor-type protein tyrosine phosphatases in mammals. Cell Signal. 2010;22:1811–7.
Mori M, Murata Y, Kotani T, Kusakari S, Ohnishi H, Saito Y, et al. Promotion of cell spreading and migration by vascular endothelial-protein tyrosine phosphatase (VE-PTP) in cooperation with integrins. J Cell Physiol. 2010;224:195–204.
Murata Y, Mori M, Kotani T, Supriatna Y, Okazawa H, Kusakari S, et al. Tyrosine phosphorylation of R3 subtype receptor-type protein tyrosine phosphatases and their complex formations with Grb2 or Fyn. Genes Cells. 2010;15:513–24.
Murata Y, Kotani T, Supriatna Y, Kitamura Y, Imada S, Kawahara K, et al. 2015 Protein tyrosine phosphatase SAP-1 protects against colitis through regulation of CEACAM20 in the intestinal epithelium. Proc Natl Acad Sci U S A. 2015;112:E4264–71.
Nagano H, Noguchi T, Inagaki K, Yoon S, Matozaki T, Itoh H, et al. Downregulation of stomach cancer-associated protein tyrosine phosphatase-1 (SAP-1) in advanced human hepatocellular carcinoma. Oncogene. 2003;22:4656–63.
Noguchi T, Tsuda M, Takeda H, Takada T, Inagaki K, Yamao T, et al. Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130cas. J Biol Chem. 2001;276:15216–24.
Pallen CJ. Protein tyrosine phosphatase α (PTPα): a Src family kinase activator and mediator of multiple biological effects. Curr Top Med Chem. 2003;3:821–35.
Peterson LW, Artis D. Intestinal epithelial cells: regulators of barrier function and immune homeostasis. Nat Rev Immunol. 2014;14:141–53.
Sadakata H, Okazawa H, Sato T, Supriatna Y, Ohnishi H, Kusakari S, et al. SAP-1 is a microvillus-specific protein tyrosine phosphatase that modulates intestinal tumorigenesis. Genes Cells. 2009;14:295–308.
Santhanam A, Peng WH, Yu YT, Sang TK, Chen GC, Meng TC. Ecdysone-induced receptor tyrosine phosphatase PTP52F regulates Drosophila midgut histolysis by enhancement of autophagy and apoptosis. Mol Cell Biol. 2014;34:1594–606.
Sato T, Soejima K, Arai E, Hamamoto J, Yasuda H, Arai D, et al. Prognostic implication of PTPRH hypomethylation in non-small cell lung cancer. Oncol Rep. 2015;34:1137–45.
Seo Y, Matozaki T, Tsuda M, Hayashi Y, Itoh H, Kasuga M. Overexpression of SAP-1, a transmembrane-type protein tyrosine phosphatase, in human colorectal cancers. Biochem Biophys Res Commun. 1997;231:705–11.
Songyang Z, Shoelson SE, Chaudhuri M, Gish G, Pawson T, Haser WG, et al. SH2 domains recognize specific phosphopeptide sequences. Cell. 1993;72:767–78.
Songyang Z, Shoelson SE, McGlade J, Olivier P, Pawson T, Bustelo XR, et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol Cell Biol. 1994;14:2777–85.
Sorkin A. Cargo recognition during clathrin-mediated endocytosis: a team effort. Curr Opin Cell Biol. 2004;16:392–9.
Takada T, Noguchi T, Inagaki K, Hosooka T, Fukunaga K, Yamao T, et al. Induction of apoptosis by stomach cancer-associated protein-tyrosine phosphatase-1. J Biol Chem. 2002;277:34359–66.
Walchli S, Espanel X, Hooft van Huijsduijnen R. Sap-1/PTPRH activity is regulated by reversible dimerization. Biochem Biophys Res Commun. 2005;331:497–502.
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this entry
Cite this entry
Murata, Y., Kotani, T., Saito, Y., Matozaki, T. (2018). PTPRH. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101831
Download citation
DOI: https://doi.org/10.1007/978-3-319-67199-4_101831
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-67198-7
Online ISBN: 978-3-319-67199-4
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences