PubMed:7559507 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":178},"obj":"Sentence"},{"id":"T2","span":{"begin":179,"end":487},"obj":"Sentence"},{"id":"T3","span":{"begin":488,"end":585},"obj":"Sentence"},{"id":"T4","span":{"begin":586,"end":1036},"obj":"Sentence"},{"id":"T5","span":{"begin":1037,"end":1300},"obj":"Sentence"},{"id":"T6","span":{"begin":1301,"end":1417},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":178},"obj":"Sentence"},{"id":"T2","span":{"begin":179,"end":487},"obj":"Sentence"},{"id":"T3","span":{"begin":488,"end":585},"obj":"Sentence"},{"id":"T4","span":{"begin":586,"end":1036},"obj":"Sentence"},{"id":"T5","span":{"begin":1037,"end":1300},"obj":"Sentence"},{"id":"T6","span":{"begin":1301,"end":1417},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Evidence for a differential interaction of SHC and the insulin receptor substrate-1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system.\nUsing the yeast two-hybrid system, a genetic assay for studying protein-protein interactions, we have examined and compared the interaction of the insulin-like growth factor-I receptor (IGF-IR) and the insulin receptor (IR) with their two known substrates p52Shc and the insulin receptor substrate-1 (IRS-1). We also mapped the specific domains of the IGF-IR and p52Shc participating in these interactions. Our findings can be summarized as follows: (i) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, (ii) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, (iii) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites (Tyr-1131, -1135, and -1136) of the IGF-IR, and (iv) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR. We propose that (i) the IGF-IR and the IR share at least in part the same molecular mechanism underlying their interplay with their two substrates, p52Shc and IRS-1, and (ii) IRS-1 interacts with the IGF-IR in a fashion that is different from that used by p52Shc. Finally, our data highlight the crucial role of the juxtamembrane domain in signaling by both the IR and the IGF-IR."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":43,"end":46},"obj":"protein"},{"id":"T2","span":{"begin":55,"end":83},"obj":"protein"},{"id":"T3","span":{"begin":85,"end":90},"obj":"protein"},{"id":"T4","span":{"begin":101,"end":146},"obj":"protein"},{"id":"T5","span":{"begin":326,"end":363},"obj":"protein"},{"id":"T6","span":{"begin":365,"end":371},"obj":"protein"},{"id":"T7","span":{"begin":381,"end":397},"obj":"protein"},{"id":"T8","span":{"begin":399,"end":401},"obj":"protein"},{"id":"T9","span":{"begin":435,"end":441},"obj":"protein"},{"id":"T10","span":{"begin":450,"end":478},"obj":"protein"},{"id":"T11","span":{"begin":480,"end":485},"obj":"protein"},{"id":"T12","span":{"begin":531,"end":537},"obj":"protein"},{"id":"T13","span":{"begin":542,"end":548},"obj":"protein"},{"id":"T14","span":{"begin":669,"end":675},"obj":"protein"},{"id":"T15","span":{"begin":714,"end":720},"obj":"protein"},{"id":"T16","span":{"begin":725,"end":730},"obj":"protein"},{"id":"T17","span":{"begin":737,"end":743},"obj":"protein"},{"id":"T18","span":{"begin":748,"end":753},"obj":"protein"},{"id":"T19","span":{"begin":766,"end":772},"obj":"protein"},{"id":"T20","span":{"begin":824,"end":830},"obj":"protein"},{"id":"T21","span":{"begin":832,"end":837},"obj":"protein"},{"id":"T22","span":{"begin":924,"end":930},"obj":"protein"},{"id":"T23","span":{"begin":970,"end":976},"obj":"protein"},{"id":"T24","span":{"begin":1018,"end":1020},"obj":"protein"},{"id":"T25","span":{"begin":1029,"end":1035},"obj":"protein"},{"id":"T26","span":{"begin":1061,"end":1067},"obj":"protein"},{"id":"T27","span":{"begin":1076,"end":1078},"obj":"protein"},{"id":"T28","span":{"begin":1185,"end":1191},"obj":"protein"},{"id":"T29","span":{"begin":1196,"end":1201},"obj":"protein"},{"id":"T30","span":{"begin":1212,"end":1217},"obj":"protein"},{"id":"T31","span":{"begin":1237,"end":1243},"obj":"protein"},{"id":"T32","span":{"begin":1293,"end":1299},"obj":"protein"},{"id":"T33","span":{"begin":1399,"end":1401},"obj":"protein"},{"id":"T34","span":{"begin":1410,"end":1416},"obj":"protein"}],"text":"Evidence for a differential interaction of SHC and the insulin receptor substrate-1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system.\nUsing the yeast two-hybrid system, a genetic assay for studying protein-protein interactions, we have examined and compared the interaction of the insulin-like growth factor-I receptor (IGF-IR) and the insulin receptor (IR) with their two known substrates p52Shc and the insulin receptor substrate-1 (IRS-1). We also mapped the specific domains of the IGF-IR and p52Shc participating in these interactions. Our findings can be summarized as follows: (i) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, (ii) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, (iii) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites (Tyr-1131, -1135, and -1136) of the IGF-IR, and (iv) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR. We propose that (i) the IGF-IR and the IR share at least in part the same molecular mechanism underlying their interplay with their two substrates, p52Shc and IRS-1, and (ii) IRS-1 interacts with the IGF-IR in a fashion that is different from that used by p52Shc. Finally, our data highlight the crucial role of the juxtamembrane domain in signaling by both the IR and the IGF-IR."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":785,"end":798},"obj":"Body_part"},{"id":"T2","span":{"begin":1353,"end":1366},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005886"}],"text":"Evidence for a differential interaction of SHC and the insulin receptor substrate-1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system.\nUsing the yeast two-hybrid system, a genetic assay for studying protein-protein interactions, we have examined and compared the interaction of the insulin-like growth factor-I receptor (IGF-IR) and the insulin receptor (IR) with their two known substrates p52Shc and the insulin receptor substrate-1 (IRS-1). We also mapped the specific domains of the IGF-IR and p52Shc participating in these interactions. Our findings can be summarized as follows: (i) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, (ii) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, (iii) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites (Tyr-1131, -1135, and -1136) of the IGF-IR, and (iv) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR. We propose that (i) the IGF-IR and the IR share at least in part the same molecular mechanism underlying their interplay with their two substrates, p52Shc and IRS-1, and (ii) IRS-1 interacts with the IGF-IR in a fashion that is different from that used by p52Shc. Finally, our data highlight the crucial role of the juxtamembrane domain in signaling by both the IR and the IGF-IR."}