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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1991-5-6
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pubmed:abstractText |
Insulin signal transmission through the plasma membrane was studied in terms of relationship between basal autophosphorylation of the beta-subunit and the ability to bind insulin by the alpha-subunit of the insulin receptor. In a cell free system, receptors phosphorylated on tyrosine residues in the absence of insulin were separated from non-phosphorylated receptors using antiphosphotyrosine antibodies. Insulin binding assays were then performed on basally autophosphorylated and on non-phosphorylated receptors. We found that the tyrosine phosphorylated receptors, which corresponded to 25% of the total number of receptors, were accountable for 60-80% of insulin binding. Scatchard representation of binding data has shown that the plot corresponding to tyrosine phosphorylated receptors was localized above, and was steeper than the plot corresponding to non-phosphorylated receptors. These data make it likely that the conformation of alpha-subunit which favours ligand binding is connected to the conformation of beta-subunit which favours phosphate reception on tyrosine residues. Reciprocally, the high-affinity conformation of insulin receptor seems to become stabilized by basal autophosphorylation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0898-6568
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
587-94
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2081098-Animals,
pubmed-meshheading:2081098-Cell Line,
pubmed-meshheading:2081098-Insulin,
pubmed-meshheading:2081098-Kinetics,
pubmed-meshheading:2081098-Phosphorylation,
pubmed-meshheading:2081098-Protein Conformation,
pubmed-meshheading:2081098-Receptor, Insulin,
pubmed-meshheading:2081098-Signal Transduction,
pubmed-meshheading:2081098-Tyrosine
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pubmed:year |
1990
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pubmed:articleTitle |
Basal autophosphorylation of insulin receptor occurs preferentially on the receptor conformation exhibiting high affinity for insulin and stabilizes this conformation.
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pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale INSERM U145. Faculté de Médecine, Nice, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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