Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-2-22
pubmed:abstractText
A search for c-Abl interacting proteins resulted in the recovery of PSTPIP1, originally identified as a binding protein of the PEST-type protein tyrosine phosphatases (PTP). PSTPIP1 was phosphorylated by c-Abl, and growth factor-induced PSTPIP1 phosphorylation was diminished in Abl null fibroblasts. PSTPIP1 was able to bridge c-Abl to the PEST-type PTPs. Several experiments suggest that the PEST-type PTPs negatively regulate c-Abl activity: c-Abl was hyperphosphorylated in PTP-PEST-deficient cells; disruption of the c-Abl-PSTPIP1-PEST-type PTP ternary complex by overexpression of PSTPIP1 mutants increased c-Abl phosphotyrosine content; and PDGF-induced c-Abl kinase activation was prolonged in PTP-PEST-deficient cells. Dephosphorylation of c-Abl by PEST-type PTP represents a novel mechanism by which c-Abl activity is regulated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-abl, http://linkedlifedata.com/resource/pubmed/chemical/Pstpip1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Ptpn12 protein, mouse
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1413-23
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11163214-Adaptor Proteins, Signal Transducing, pubmed-meshheading:11163214-Animals, pubmed-meshheading:11163214-COS Cells, pubmed-meshheading:11163214-Carrier Proteins, pubmed-meshheading:11163214-Cells, Cultured, pubmed-meshheading:11163214-Cytoskeletal Proteins, pubmed-meshheading:11163214-Enzyme Activation, pubmed-meshheading:11163214-Epitopes, pubmed-meshheading:11163214-Macromolecular Substances, pubmed-meshheading:11163214-Mice, pubmed-meshheading:11163214-Mutation, pubmed-meshheading:11163214-Phosphorylation, pubmed-meshheading:11163214-Phosphotyrosine, pubmed-meshheading:11163214-Platelet-Derived Growth Factor, pubmed-meshheading:11163214-Protein Binding, pubmed-meshheading:11163214-Protein Tyrosine Phosphatase, Non-Receptor Type 12, pubmed-meshheading:11163214-Protein Tyrosine Phosphatases, pubmed-meshheading:11163214-Proto-Oncogene Proteins c-abl, pubmed-meshheading:11163214-Substrate Specificity, pubmed-meshheading:11163214-Transfection, pubmed-meshheading:11163214-Two-Hybrid System Techniques, pubmed-meshheading:11163214-Yeasts, pubmed-meshheading:11163214-src Homology Domains
pubmed:year
2000
pubmed:articleTitle
Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't