Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST

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Published in:	Molecular and Cellular Biology Vol. 16; no. 11; pp. 6408 - 6418
Main Authors:	Garton, A J, Flint, A J, Tonks, N K
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-11-1996
Subjects:	Animals COS Cells Crk-Associated Substrate Protein Cytosol - enzymology Enzyme Inhibitors - pharmacology HeLa Cells Humans Kinetics Mammals Mutagenesis, Site-Directed Phosphoproteins - metabolism Point Mutation Protein Tyrosine Phosphatase, Non-Receptor Type 12 Protein Tyrosine Phosphatases - antagonists & inhibitors Protein Tyrosine Phosphatases - metabolism Proteins Recombinant Proteins - metabolism Retinoblastoma Protein - metabolism Retinoblastoma-Like Protein p130 Substrate Specificity Transfection Tumor Cells, Cultured Vanadates - pharmacology
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Abstract	Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
AbstractList	PTP-PEST is a ubiquitously expressed, cytosolic, mammalian protein tyrosine phosphatase (PTP) which exhibits high specific activity in vitro. We have investigated the substrate specificity of PTP-PEST by a novel substrate-trapping approach in combination with in vitro dephosphorylation experiments. We initially identified a prominent 130-kDa tyrosine-phosphorylated protein in pervanadate-treated HeLa cell lysates which was preferentially dephosphorylated by PTP-PEST in vitro. In order to identify this potential substrate, mutant (substrate-trapping) forms of PTP-PEST were generated which lack catalytic activity but retain the ability to bind substrates. These mutant proteins associated in stable complexes exclusively with the same 130-kDa protein, which was identified as p130(cas) by immunoblotting. This exclusive association was observed in lysates from several cell lines and in transfected COS cells, but was not observed with other members of the PTP family, strongly suggesting that p130(cas) represents a major physiologically relevant substrate for PTP-PEST. Our studies suggest potential roles for PTP-PEST in regulation of p130(cas) function. These functions include mitogen- and cell adhesion-induced signalling events and probable roles in transformation by various oncogenes. These results provide the first demonstration of a PTP having an inherently restricted substrate specificity in vitro and in vivo. The methods used to identify p130(cas) as a specific substrate for PTP-PEST are potentially applicable to any PTP and should therefore prove useful in determining the physiological substrates of other members of the PTP family. Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
Author	N K Tonks A J Garton A J Flint
AuthorAffiliation	Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724-2208, USA
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BackLink	https://www.ncbi.nlm.nih.gov/pubmed/8887669$$D View this record in MEDLINE/PubMed
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Snippet	Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... PTP-PEST is a ubiquitously expressed, cytosolic, mammalian protein tyrosine phosphatase (PTP) which exhibits high specific activity in vitro. We have...
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StartPage	6408
SubjectTerms	Animals COS Cells Crk-Associated Substrate Protein Cytosol - enzymology Enzyme Inhibitors - pharmacology HeLa Cells Humans Kinetics Mammals Mutagenesis, Site-Directed Phosphoproteins - metabolism Point Mutation Protein Tyrosine Phosphatase, Non-Receptor Type 12 Protein Tyrosine Phosphatases - antagonists & inhibitors Protein Tyrosine Phosphatases - metabolism Proteins Recombinant Proteins - metabolism Retinoblastoma Protein - metabolism Retinoblastoma-Like Protein p130 Substrate Specificity Transfection Tumor Cells, Cultured Vanadates - pharmacology
Title	Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST
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