Expression, localization, and biological function of the R3 subtype of receptor-type protein tyrosine phosphatases in mammals

Cellular Signalling
Takashi MatozakiHiroshi Ohnishi

Abstract

The R3 subtype of receptor-type protein tyrosine phosphatases (RPTPs) includes VE-PTP, DEP-1, PTPRO, and SAP-1. All of these enzymes share a similar structure, with a single catalytic domain and putative tyrosine phosphorylation sites in the cytoplasmic region and fibronectin type III-like domains in the extracellular region. The expression of each R3 RPTP is largely restricted to a single or limited number of cell types, with VE-PTP and DEP-1 being expressed in endothelial or hematopoietic cells, PTPRO in neurons and in podocytes of the renal glomerulus, and SAP-1 in gastrointestinal epithelial cells. In addition, these RPTPs are localized specifically at the apical surface of polarized cells. The structure, expression, and localization of the R3 RPTPs suggest that they perform tissue-specific functions and that they might act through a common mechanism that includes activation of Src family kinases. In this review, we describe recent insights into R3-subtype RPTPs, particularly those of mammals.

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Citations

May 6, 2011·The Journal of Biological Chemistry·Ondrej StepanekTomas Brdicka
Mar 22, 2013·The Journal of Neuroscience : the Official Journal of the Society for Neuroscience·Graziana GattoRüdiger Klein
Jul 3, 2015·Oncology Reports·Takashi SatoTomoko Betsuyaku
Jul 22, 2015·Proceedings of the National Academy of Sciences of the United States of America·Yoji MurataTakashi Matozaki
Mar 22, 2012·Cell Cycle·Kunimasa YanHitoshi Takenaka
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Oct 6, 2016·Expert Review of Gastroenterology & Hepatology·Takenori KotaniTakashi Matozaki
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Apr 8, 2017·American Journal of Physiology. Lung Cellular and Molecular Physiology·Dheeraj SoniChinnaswamy Tiruppathi
Oct 24, 2014·The Journal of Immunology : Official Journal of the American Association of Immunologists·Runqiu JiangBeicheng Sun

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