Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

PTPRH

  • Yoji MurataEmail author
  • Takenori Kotani
  • Yasuyuki Saito
  • Takashi MatozakiEmail author
Reference work entry
First Online:
DOI: https://doi.org/10.1007/978-3-319-67199-4_101831
How to cite

Synonyms

 Protein tyrosine phosphatase, receptor type H;  R-PTP-H;  Receptor-type tyrosine-protein phosphatase H;  SAP-1;  Sap-1;  SAP1;  Stomach cancer-associated protein tyrosine phosphatase 1

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...
This is a preview of subscription content, log in to check access.

References

  1. 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.CrossRefPubMedGoogle Scholar
  2. Clarke AR. Wnt signalling in the mouse intestine. Oncogene. 2006;25:7512–21.CrossRefPubMedGoogle Scholar
  3. den Hertog J, Östman A, Böhmer FD. Protein tyrosine phosphatases: regulatory mechanisms. FEBS J. 2008;275:831–47.CrossRefGoogle Scholar
  4. 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.CrossRefPubMedGoogle Scholar
  5. 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.PubMedGoogle Scholar
  6. 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.CrossRefPubMedGoogle Scholar
  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.PubMedGoogle Scholar
  8. 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.PubMedGoogle Scholar
  9. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  10. 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.CrossRefPubMedGoogle Scholar
  11. 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.CrossRefPubMedGoogle Scholar
  12. 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.CrossRefPubMedGoogle Scholar
  13. Peterson LW, Artis D. Intestinal epithelial cells: regulators of barrier function and immune homeostasis. Nat Rev Immunol. 2014;14:141–53.CrossRefPubMedGoogle Scholar
  14. 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.CrossRefPubMedGoogle Scholar
  15. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  16. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  17. 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.CrossRefPubMedGoogle Scholar
  18. 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.CrossRefPubMedGoogle Scholar
  19. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  20. Sorkin A. Cargo recognition during clathrin-mediated endocytosis: a team effort. Curr Opin Cell Biol. 2004;16:392–9.CrossRefPubMedGoogle Scholar
  21. 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.CrossRefPubMedGoogle Scholar
  22. 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.CrossRefPubMedGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Division of Molecular and Cellular Signaling, Department of Biochemistry and Molecular BiologyKobe University Graduate School of MedicineKobeJapan