Single-molecule functional anatomy of endogenous HER2-HER3 heterodimers
- Title
- Single-molecule functional anatomy of endogenous HER2-HER3 heterodimers
- Author
- 채필석
- Issue Date
- 2020-05
- Publisher
- ELIFE SCIENCES PUBLICATIONS LTD
- Citation
- ELIFE, v. 9, Article no. e53934, 22pp
- 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.
- URI
- https://elifesciences.org/articles/53934https://repository.hanyang.ac.kr/handle/20.500.11754/164463
- ISSN
- 2050-084X
- DOI
- 10.7554/eLife.53934
- Appears in Collections:
- COLLEGE OF ENGINEERING SCIENCES[E](공학대학) > BIONANO ENGINEERING(생명나노공학과) > Articles
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