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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1998-11-6
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pubmed:abstractText |
The oncogenic Bcr-Abl variant of the c-Abl tyrosine kinase transforms cells by a mechanism dependent on activation of the stress-activated protein kinase (SAPK). Other work has shown that c-Abl interacts with the SHPTP1 protein tyrosine phosphatase in induction of SAPK activity by genotoxic stress. The present studies demonstrate that Bcr-Abl binds constitutively to SHPTP1. We show that Bcr-Abl phosphorylates SHPTP1 on C-terminal Y536 and Y564 sites. The functional significance of the Bcr-Abl/SHPTP1 interaction is supported by the finding that SHPTP1 regulates Bcr-Abl-induced SAPK activity. Importantly, SHPTP1 also decreases Bcr-Abl-dependent transformation of fibroblasts. These findings indicate that SHPTP1 functions as a tumor suppressor in cells transformed by Bcr-Abl.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Fusion Proteins, bcr-abl,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn6 protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1889-92
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9788431-3T3 Cells,
pubmed-meshheading:9788431-Animals,
pubmed-meshheading:9788431-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9788431-Cell Line, Transformed,
pubmed-meshheading:9788431-Cell Transformation, Neoplastic,
pubmed-meshheading:9788431-Down-Regulation,
pubmed-meshheading:9788431-Enzyme Induction,
pubmed-meshheading:9788431-Fusion Proteins, bcr-abl,
pubmed-meshheading:9788431-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9788431-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:9788431-Mice,
pubmed-meshheading:9788431-Mitogen-Activated Protein Kinases,
pubmed-meshheading:9788431-Phosphorylation,
pubmed-meshheading:9788431-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:9788431-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:9788431-Protein Tyrosine Phosphatases
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pubmed:year |
1998
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pubmed:articleTitle |
Regulation of Bcr-Abl-induced SAP kinase activity and transformation by the SHPTP1 protein tyrosine phosphatase.
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pubmed:affiliation |
Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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