NDLI: Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that can regulate cell survival and proliferation.

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Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that can regulate cell survival and proliferation.

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Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that can regulate cell survival and proliferation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Seifert, R. A. Bowen-pope, D. F. Coats, S. A. Wright, M. B. Daum, G. Oganesian, A. Poot, M.
Description	Author Affiliation: Oganesian A ( Department of Pathology, University of Washington, Seattle, WA 98195, USA.);
Abstract	Protein tyrosine phosphatase RQ (PTPRQ) was initially identified as a protein tyrosine phosphatase (PTPase)-like protein that is upregulated in a model of renal injury. Here we present evidence that, like PTEN, the biologically important enzymatic activity of PTPRQ is as a phosphatidylinositol phosphatase (PIPase). The PIPase specificity of PTPRQ is broader than that of PTEN and depends on different amino acid residues in the catalytic domain. In vitro, the recombinant catalytic domain of PTPRQ has low PTPase activity against tyrosine-phosphorylated peptide and protein substrates but can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. PTPRQ does not have either of the basic amino acids in the catalytic domain that are important for the PIPase activity of PTEN or the sequence motifs that are characteristic of type II phosphatidylinositol 5-phosphatases. Instead, the PIPase activity depends on the WPE sequence present in the catalytic cleft of PTPRQ, and in the 'inactive' D2 domains of many dual-domain PTPases, in place of the WPD motif present in standard active PTPases. Overexpression of PTPRQ in cultured cells inhibits proliferation and induces apoptosis. An E2171D mutation that retains or increases PTPase activity but eliminates PIPase activity, eliminates the inhibitory effects on proliferation and apoptosis. These results indicate that PTPRQ represents a subtype of the PTPases whose biological activities result from its PIPase activity rather than its PTPase activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Phosphoric Monoester Hydrolases Chemistry Protein Tyrosine Phosphatases Physiology Protein-Serine-Threonine Kinases Animals Apoptosis Catalytic Domain Cell Division Cell Survival DNA Metabolism Dose-Response Relationship, Drug Genetic Vectors Glutathione Transferase Hydrolysis Membrane Potentials Mitochondria Phosphatidylinositol Phosphates Phosphorylation Protein Structure, Tertiary Proto-Oncogene Proteins Proto-Oncogene Proteins C-akt Receptor-Like Protein Tyrosine Phosphatases, Class 3 Recombinant Fusion Proteins Transfection Tumor Cells, Cultured Tyrosine Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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