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rdf:type |
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lifeskim:mentions |
umls-concept:C0026882,
umls-concept:C0031715,
umls-concept:C0034818,
umls-concept:C0041485,
umls-concept:C0178666,
umls-concept:C0206131,
umls-concept:C0381451,
umls-concept:C1514562,
umls-concept:C1622525,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
17
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pubmed:dateCreated |
1999-5-20
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pubmed:abstractText |
CSF-1 is equipotent to insulin in its ability to stimulate 2-[3H]deoxyglucose uptake in 3T3-L1 adipocytes expressing the colony stimulating factor-1 receptor/insulin receptor chimera (CSF1R/IR). However, CSF-1-stimulated glucose uptake and glycogen synthesis is reduced by 50% in comparison to insulin in 3T3-L1 cells expressing a CSF1R/IR mutated at Tyr960 (CSF1R/IRA960). CSF-1-treated adipocytes expressing the CSF1R/IRA960 were impaired in their ability to phosphorylate insulin receptor substrate 1 (IRS-1) but not in their ability to phosphorylate IRS-2. Immunoprecipitation of IRS proteins followed by Western blotting revealed that the intact CSF1R/IR co-precipitates with IRS-2 from CSF-1-treated cells. In contrast, the CSF1R/IRA960 co-precipitates poorly with IRS-2. These observations suggest that Tyr960 is important for interaction of the insulin receptor cytoplasmic domain with IRS-2, but it is not essential to the ability of the insulin receptor tyrosine kinase to use IRS-2 as a substrate. These observations also suggest that in 3T3-L1 adipocytes, tyrosine phosphorylation of IRS-2 by the insulin receptor tyrosine kinase is not sufficient for maximal stimulation of receptor-regulated glucose transport or glycogen synthesis.
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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/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin Receptor Substrate Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Irs2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Macrophage Colony-Stimulating Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12075-80
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10207032-3T3 Cells,
pubmed-meshheading:10207032-Adipocytes,
pubmed-meshheading:10207032-Animals,
pubmed-meshheading:10207032-Biological Transport,
pubmed-meshheading:10207032-Cell Membrane,
pubmed-meshheading:10207032-Cytoplasm,
pubmed-meshheading:10207032-Enzyme Activation,
pubmed-meshheading:10207032-Glucose,
pubmed-meshheading:10207032-Insulin Receptor Substrate Proteins,
pubmed-meshheading:10207032-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10207032-Ligands,
pubmed-meshheading:10207032-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:10207032-Mice,
pubmed-meshheading:10207032-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:10207032-Phosphoproteins,
pubmed-meshheading:10207032-Phosphorylation,
pubmed-meshheading:10207032-Receptor, Insulin,
pubmed-meshheading:10207032-Receptor, Macrophage Colony-Stimulating Factor,
pubmed-meshheading:10207032-Recombinant Fusion Proteins,
pubmed-meshheading:10207032-Tyrosine
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pubmed:year |
1999
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pubmed:articleTitle |
Mutation of tyrosine 960 within the insulin receptor juxtamembrane domain impairs glucose transport but does not inhibit ligand-mediated phosphorylation of insulin receptor substrate-2 in 3T3-L1 adipocytes.
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pubmed:affiliation |
Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198-6805, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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