Abstract:
:We have tested the hypothesis that activation of the insulin receptor tyrosine kinase is due to autophosphorylation of tyrosines 1146, 1150 and 1151 within a putative autoinhibitory domain. A synthetic peptide corresponding to residues 1134-1162, with tyrosines substituted by alanine or phenylalanine, of the insulin receptor beta subunit was tested for its inhibitory potency and specificity towards the tyrosine kinase activity. This synthetic peptide gave inhibition of the insulin receptor tyrosine kinase autophosphorylation and phosphorylation of the exogenous substrate poly(Glu, Tyr) with an approximate IC50 of 100 microM. Inhibition appeared to be independent of the concentrations of insulin or the substrate poly(Glu, Tyr) but was decreased by increasing concentrations of ATP. This same peptide also inhibited the EGF receptor tyrosine kinase but not a serine/threonine protein kinase. These results are consistent with the hypothesis that this autophosphorylation domain contains an autoinhibitory sequence.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Filipek A,Soderling TRdoi
10.1007/BF00926082subject
Has Abstractpub_date
1993-03-24 00:00:00pages
103-10issue
2eissn
0300-8177issn
1573-4919journal_volume
120pub_type
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