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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0018270,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0085536,
umls-concept:C0221920,
umls-concept:C0475264,
umls-concept:C1335283,
umls-concept:C1335872,
umls-concept:C1705637,
umls-concept:C1879547
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pubmed:issue |
4
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pubmed:dateCreated |
2000-8-8
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pubmed:abstractText |
The SH2 domain protein-tyrosine phosphatase SHP-1 has been shown earlier to bind to the epidermal growth factor receptor and to have the capacity for receptor dephosphorylation. New bi- and tricistronic expression vectors (pNRTIS-21 and pNRTIS-33, respectively) based on the tetracycline system were constructed and employed to generate stable cell lines with inducible expression of SHP-1. Inducible overexpression of SHP-1 in A431 cells led to attenuation of epidermal growth factor (EGF) receptor autophosphorylation and of EGF-induced DNA binding of 'signal transducers and activators of transcription' (STAT) 1 and 3. SHP-1 was localized in the cytoplasm with an enrichment in the perinuclear compartment. Association of SHP-1 with perinuclear structures may form the basis for a partial cofractionation with nuclei observed in different types of transfected cells and also with endogenous SHP-1 in U-937 cells. Treatment of SHP-1-overexpressing A431 cells or of HaCaT human keratinocytes expressing SHP-1 endogenously with the Ca2+-ionophore A23187 resulted in partial nuclear accumulation of SHP-1. Thus, SHP-1 may interact with substrates or regulatory proteins in perinuclear or nuclear structures.
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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/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ionophores,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors,
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,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/SH2 Domain-Containing Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Stat1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Stat3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Tetracycline,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0171-9335
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
261-71
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10826494-3T3 Cells,
pubmed-meshheading:10826494-Animals,
pubmed-meshheading:10826494-Calcimycin,
pubmed-meshheading:10826494-Cell Line,
pubmed-meshheading:10826494-Cell Nucleus,
pubmed-meshheading:10826494-DNA, Complementary,
pubmed-meshheading:10826494-DNA-Binding Proteins,
pubmed-meshheading:10826494-Enzyme Activation,
pubmed-meshheading:10826494-Epidermal Growth Factor,
pubmed-meshheading:10826494-Humans,
pubmed-meshheading:10826494-Immunohistochemistry,
pubmed-meshheading:10826494-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10826494-Ionophores,
pubmed-meshheading:10826494-Keratinocytes,
pubmed-meshheading:10826494-Mice,
pubmed-meshheading:10826494-Protein Structure, Tertiary,
pubmed-meshheading:10826494-Protein Synthesis Inhibitors,
pubmed-meshheading:10826494-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:10826494-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:10826494-Protein Tyrosine Phosphatases,
pubmed-meshheading:10826494-Receptor, Epidermal Growth Factor,
pubmed-meshheading:10826494-SH2 Domain-Containing Protein Tyrosine Phosphatases,
pubmed-meshheading:10826494-STAT1 Transcription Factor,
pubmed-meshheading:10826494-STAT3 Transcription Factor,
pubmed-meshheading:10826494-Signal Transduction,
pubmed-meshheading:10826494-Tetracycline,
pubmed-meshheading:10826494-Trans-Activators,
pubmed-meshheading:10826494-Transfection,
pubmed-meshheading:10826494-src Homology Domains
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pubmed:year |
2000
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pubmed:articleTitle |
Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells.
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pubmed:affiliation |
Research Unit Molecular Cell Biology, Medical Faculty, Friedrich Schiller University, Jena, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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