Evidence map›Paper›PMID 32267234›Full record

ArticleeLife2020

Single-molecule functional anatomy of endogenous HER2-HER3 heterodimers.

Byoungsan Choi, Minkwon Cha, Gee Sung Eun, Dae Hee Lee, Seul Lee, Muhammad Ehsan, Pil Seok Chae, Won Do Heo, YongKeun Park, Tae-Young Yoon

Abstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Emerging Targets in Non-Small Cell Lung Cancer.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Signaling pathways and therapeutic interventions in gastric cancer.Signal transduction and targeted therapy · 2022
    Review
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Byoungsan Choi *School of Biological Sciences and Institute for Molecular Biology and Genetics, Seoul National University, Seoul, Republic of Korea.ORCID https://orcid.org/0000-0002-9679-4233
Minkwon Cha *Department of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Republic of Korea.ORCID https://orcid.org/0000-0003-2316-8984
Gee Sung EunSchool of Biological Sciences and Institute for Molecular Biology and Genetics, Seoul National University, Seoul, Republic of Korea.
Dae Hee LeeProteina Co. Ltd., Seoul, Republic of Korea.
Seul LeeProteina Co. Ltd., Seoul, Republic of Korea.
Muhammad EhsanDepartment of Bionanotechnology, Hanyang University, Ansan, Republic of Korea.
Pil Seok ChaeDepartment of Bionanotechnology, Hanyang University, Ansan, Republic of Korea.
Won Do HeoDepartment of Biological Sciences, KAIST, Daejeon, Republic of Korea.
YongKeun ParkDepartment of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Republic of Korea.ORCID http://orcid.org/0000-0003-0528-6661
Tae-Young YoonSchool of Biological Sciences and Institute for Molecular Biology and Genetics, Seoul National University, Seoul, Republic of Korea.ORCID https://orcid.org/0000-0002-5184-7725

Funding

National Research Foundation of Korea NRF-2011-0018352
6 · The paper itself

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.

Indexed as

Signal TransductionDimerizationErb-b2 Receptor Tyrosine KinasesHEK293 CellsHumansModels, MolecularPhosphorylationProtein ConformationProtein DomainsReceptor, ErbB-3Single Molecule ImagingTyrosineErb-b2 Receptor Tyrosine KinasesReceptor, ErbB-3Tyrosinebiochemistrycatalytic ratechemical biologyhumanprotein interactionreceptor tyrosine kinasetyrosine phosphorylation

Identifiers

PMID32267234
PMCPMC7176432

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.