PubMed:7589433 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":15,"end":18},"obj":"protein"},{"id":"T2","span":{"begin":30,"end":41},"obj":"protein"},{"id":"T3","span":{"begin":47,"end":54},"obj":"protein"},{"id":"T4","span":{"begin":59,"end":64},"obj":"protein"},{"id":"T5","span":{"begin":135,"end":138},"obj":"protein"},{"id":"T6","span":{"begin":150,"end":161},"obj":"protein"},{"id":"T7","span":{"begin":171,"end":187},"obj":"protein"},{"id":"T8","span":{"begin":189,"end":191},"obj":"protein"},{"id":"T9","span":{"begin":201,"end":215},"obj":"protein"},{"id":"T10","span":{"begin":217,"end":223},"obj":"protein"},{"id":"T11","span":{"begin":420,"end":422},"obj":"protein"},{"id":"T12","span":{"begin":427,"end":433},"obj":"protein"},{"id":"T13","span":{"begin":438,"end":441},"obj":"protein"},{"id":"T14","span":{"begin":546,"end":549},"obj":"protein"},{"id":"T15","span":{"begin":590,"end":597},"obj":"protein"},{"id":"T16","span":{"begin":602,"end":613},"obj":"protein"},{"id":"T17","span":{"begin":664,"end":671},"obj":"protein"},{"id":"T18","span":{"begin":688,"end":691},"obj":"protein"},{"id":"T19","span":{"begin":709,"end":716},"obj":"protein"},{"id":"T20","span":{"begin":718,"end":728},"obj":"protein"},{"id":"T21","span":{"begin":733,"end":744},"obj":"protein"},{"id":"T22","span":{"begin":745,"end":755},"obj":"protein"},{"id":"T23","span":{"begin":935,"end":937},"obj":"protein"},{"id":"T24","span":{"begin":952,"end":958},"obj":"protein"},{"id":"T25","span":{"begin":999,"end":1002},"obj":"protein"},{"id":"T26","span":{"begin":1008,"end":1015},"obj":"protein"},{"id":"T27","span":{"begin":1016,"end":1026},"obj":"protein"},{"id":"T28","span":{"begin":1059,"end":1066},"obj":"protein"},{"id":"T29","span":{"begin":1089,"end":1092},"obj":"protein"},{"id":"T30","span":{"begin":1097,"end":1108},"obj":"protein"},{"id":"T31","span":{"begin":1140,"end":1147},"obj":"protein"},{"id":"T32","span":{"begin":1188,"end":1199},"obj":"protein"},{"id":"T33","span":{"begin":1201,"end":1210},"obj":"protein"},{"id":"T34","span":{"begin":1245,"end":1251},"obj":"protein"},{"id":"T35","span":{"begin":1302,"end":1305},"obj":"protein"},{"id":"T36","span":{"begin":1385,"end":1396},"obj":"protein"}],"text":"Interaction of p85 subunit of PI 3-kinase with insulin and IGF-1 receptors analysed by using the two-hybrid system.\nInteraction of the p85 subunit of PI 3-kinase with the insulin receptor (IR) and the IGF-1 receptor (IGF-1R) was investigated using the two-hybrid system by assessing for his3 and lacZ activation in S. cerevisiae. The experiments were performed with the cytoplasmic beta domain (wild type or mutated) of IR and IGF-1R and p85 or its subdomains (N + C-SH2, N-SH2, C-SH2, SH3 + N-SH2). The results of his3 activation indicated that p85, N + C-SH2 and C-SH2 interact with both IR beta and IGF-1R beta, whereas N-SH2 and SH3 + N-SH2 interact only with IR beta. Interaction of p85 and N+C-SH2 with IR beta (delta C-43) or IGF-1R beta(delta C-43) in which the C-terminal 43 amino acids (including the YXXM motif) were deleted, persisted. The internal binding site thus revealed was not altered by further mutating Y960/F for IR or Y950/F for IGF-1R. Activation of lacZ upon interaction of p85 with IR beta(delta C-43) was 4-fold less as compared to IR beta. This activation with p85 and IGF-1R beta was 4-fold less as compared to IR beta and was somewhat increased (2-fold) for IGF-1R beta (delta C-43). Thus, the C-terminal domain in IGF-1R appears to exert a negative control on binding of p85 thereby providing a possible regulatory mechanism for direct activation of the PI 3-kinase pathway."}