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HERO ID
2053270
Reference Type
Journal Article
Subtype
Review
Title
Expression, localization, and biological function of the R3 subtype of receptor-type protein tyrosine phosphatases in mammals
Author(s)
Matozaki, T; Murata, Y; Mori, M; Kotani, T; Okazawa, H; Ohnishi, H
Year
2010
Is Peer Reviewed?
Yes
Journal
Cellular Signalling
ISSN:
0898-6568
Volume
22
Issue
12
Page Numbers
1811-1817
Language
English
PMID
20633639
DOI
10.1016/j.cellsig.2010.07.001
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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