Single-molecule functional anatomy of endogenous HER2-HER3 heterodimers
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Choi, Byoungsan | - |
dc.contributor.author | Cha, Minkwon | - |
dc.contributor.author | Bun, Gee Sung | - |
dc.contributor.author | Lee, Dae Hee | - |
dc.contributor.author | Lee, Seul | - |
dc.contributor.author | Ehsan, Muhammad | - |
dc.contributor.author | Chae, Pil Seok | - |
dc.contributor.author | Heo, Won Do | - |
dc.contributor.author | Park, YongKeun | - |
dc.contributor.author | Yoon, Tae-Young | - |
dc.date.accessioned | 2021-06-22T09:05:17Z | - |
dc.date.available | 2021-06-22T09:05:17Z | - |
dc.date.created | 2021-01-21 | - |
dc.date.issued | 2020-04 | - |
dc.identifier.issn | 2050-084X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/1171 | - |
dc.description.abstract | Human epidermal growth factor receptors (HERs) are the primary targets of many directed cancer therapies. However, the reason a specific dimer of HERs generates a stronger proliferative signal than other permutations remains unclear. Here, we used single-molecule immunoprecipitation to develop a biochemical assay for endogenously-formed, entire HER2-HER3 heterodimers. We observed unexpected, large conformational fluctuations in juxta-membrane and kinase domains of the HER2-HER3 heterodimer. Nevertheless, the individual HER2-HER3 heterodimers catalyze tyrosine phosphorylation at an unusually high rate, while simultaneously interacting with multiple copies of downstream signaling effectors. Our results suggest that the high catalytic rate and multi-tasking capability make a concerted contribution to the strong signaling potency of the HER2-HER3 heterodimers. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ELIFE SCIENCES PUBLICATIONS LTD | - |
dc.title | Single-molecule functional anatomy of endogenous HER2-HER3 heterodimers | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chae, Pil Seok | - |
dc.identifier.doi | 10.7554/eLife.53934 | - |
dc.identifier.scopusid | 2-s2.0-85083914083 | - |
dc.identifier.wosid | 000529338200001 | - |
dc.identifier.bibliographicCitation | ELIFE, v.9, pp.1 - 22 | - |
dc.relation.isPartOf | ELIFE | - |
dc.citation.title | ELIFE | - |
dc.citation.volume | 9 | - |
dc.citation.startPage | 1 | - |
dc.citation.endPage | 22 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Life Sciences & Biomedicine - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Biology | - |
dc.subject.keywordPlus | EPIDERMAL-GROWTH-FACTOR | - |
dc.subject.keywordPlus | CELL LUNG-CANCER | - |
dc.subject.keywordPlus | FACTOR RECEPTOR | - |
dc.subject.keywordPlus | EXTRACELLULAR REGION | - |
dc.subject.keywordPlus | MONOCLONAL-ANTIBODY | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | ERBB RECEPTORS | - |
dc.subject.keywordPlus | BREAST-CANCER | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | EGF | - |
dc.identifier.url | https://www.scopus.com/record/display.uri?eid=2-s2.0-85083914083&origin=inward&txGid=dc07966e93e097afac51bc55a39d530a | - |
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