Tyrosine phosphorylation of Ras GTPase-activating protein stabilizes its association with p62 at membranes of v-Src transformed cells
DC Field | Value | Language |
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dc.contributor.author | PARK, S (PARK, S) | - |
dc.contributor.author | JOVE, R (JOVE, R) | - |
dc.date.accessioned | 2022-04-19T14:04:55Z | - |
dc.date.available | 2022-04-19T14:04:55Z | - |
dc.date.issued | 1993-12 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/151014 | - |
dc.description.abstract | Ras GTPase-activating protein (GAP) regulates the activity of Ras proteins, which have key roles in signal transduction pathways downstream of oncogenic and receptor tyrosine kinases. Previous studies indicated that Tyr-457 of bovine GAP (Tyr-460 of human GAP) is the major site of phosphorylation by viral Src (v-Src) kinase and epidermal growth factor receptor. The finding that Tyr-457 in GAP is located immediately adjacent to Src homology 2 (SH2) and 3 (SH3) domains led us to investigate the possibility that this specific phosphorylation regulates protein-protein interactions involving GAP. For this purpose, we constructed a full-length GAP mutant containing a substitution of Phe-457 in place of Tyr-457. Both wild-type GAP and mutant GAP(F457) were tagged with the KT3 epitope at the carboxyl terminus and were expressed in v-Src transformed rat fibroblasts. In vivo phosphorylation analyses established that GAP(F457) was weakly phosphorylated on tyrosine and, as expected, lacked the phosphopeptide containing Tyr-457. Analysis of GAP-associated proteins in anti-KT3 immunoprecipitates showed that GAP stably associated with two major phosphoproteins, p62 and p190, which have been previously described. Significantly, association of p62 with GAP(F457) was reduced approximately 3-fold compared with wild-type GAP. Subce | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Tyrosine phosphorylation of Ras GTPase-activating protein stabilizes its association with p62 at membranes of v-Src transformed cells | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1016/S0021-9258(19)74450-0 | - |
dc.identifier.scopusid | 2-s2.0-0027378333 | - |
dc.identifier.wosid | A1993MK10000066 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.268, no.34, pp 25728 - 25734 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 268 | - |
dc.citation.number | 34 | - |
dc.citation.startPage | 25728 | - |
dc.citation.endPage | 25734 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S0021925819744500 | - |
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