Insulin receptor is an oligomeric protein, its "beta" subunit possessing insulin-stimulated tyrosine kinase activity that causes its autophosphorylation. "In vivo", insulin receptor is also phosphorylated on serine and threonine in a reaction catalyzed by extrinsic protein kinases. Phosphorylation on these residues seems to affect the response of the receptor to the presence of insulin. The aim of this project is to unravel the role of casein kinases 1 and 2 on the phosphorylation of rat hepatic insulin receptor. The possible relevance of the phosphorylation by these enzymes on the affinity for insulin, tyrosine kinase activity and state of aggregation of the receptor will be studied because of their importance in the transmission of the hormonal signal. The importance of the serine/threonine phosphorylation on the impaired insulin receptor functioning associated to streptozoticin-induce
|Effective start/end date||4/10/90 → 4/10/93|
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