Evidence map›Paper›PMID 42054992›Full record

ArticleCell2026

ErbB family receptor dimerization dynamics and dysregulation via long-term single-molecule imaging.

Kaibo Ma, Xiaojie Ma, João F Shida, Zijian Niu, Yuzhu Karlie Lin, Saptarshi Mandal, Alexandra Dobbins, Lior Golomb, Michael J Eck, Heidi Greulich and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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

12 authors.

Kaibo MaBroad Institute of MIT and Harvard, Cambridge, MA, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.
Xiaojie MaBroad Institute of MIT and Harvard, Cambridge, MA, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
João F ShidaBroad Institute of MIT and Harvard, Cambridge, MA, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Zijian NiuBroad Institute of MIT and Harvard, Cambridge, MA, USA; Computational and Systems Biology Program, Massachusetts Institute of Technology, Cambridge, MA, USA.
Yuzhu Karlie LinBroad Institute of MIT and Harvard, Cambridge, MA, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Saptarshi MandalBroad Institute of MIT and Harvard, Cambridge, MA, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Alexandra DobbinsDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA, USA.
Lior GolombDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA, USA.
Michael J EckDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Heidi GreulichDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA, USA; Cancer Program, Broad Institute of Harvard and MIT, Cambridge, MA, USA.
Matthew MeyersonDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA, USA; Cancer Program, Broad Institute of Harvard and MIT, Cambridge, MA, USA; Department of Genetics, Harvard Medical School, Boston, MA, USA.
Chunte Sam PengBroad Institute of MIT and Harvard, Cambridge, MA, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA. Electronic address: sampeng@mit.edu.

Funding

Ultralong-term single-molecule imaging of amyloid precursor protein (APP) processing in Alzheimer's diseaseR00AG065516 · NIA · BROAD INSTITUTE, INC. · PI PENG, CHUNTE · 2023 to 2025
$722k
NIA NIH HHS R00 AG065516
6 · The paper itself

Abstract

Dimerization is crucial for the activation of ErbB family receptors, yet the real-time dynamics and effects of oncogenic mutations remain unclear. Here, we performed long-term, multicolor single-particle tracking (SPT) of EGFR, HER2, and HER3 in living cells using upconverting nanoparticles (UCNPs), which do not photobleach. Our technique enables continuous observation of receptor interactions, revealing details of their dimerization dynamics. Oncogenic EGFR mutations promote stable, ligand-independent dimerization. Unexpectedly, both HER2 and HER3 exhibit constitutive homodimerization, prompting a revised model for their activation mechanisms. HER2 mutations modestly enhance homodimer stability compared with EGFR mutations, while HER3 mutations destabilize homodimers, suggesting that HER3 homodimerization sequesters HER3 and limits heterodimerization with other receptors. We also identified stable, ligand-independent heterodimers among all three receptors, further stabilized by ligand stimulation. These insights offer a comprehensive ErbB interaction network, elucidating diverse dimerization mechanisms and implications for oncogenic signaling.

Indexed as

Erb-b2 Receptor Tyrosine KinasesErbB ReceptorsReceptor, ErbB-3Single Molecule ImagingAnimalsHumansLigandsMutationNanoparticlesProtein MultimerizationSignal TransductionERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesERBB3 protein, humanErbB ReceptorsLigandsReceptor, ErbB-3dimerization networkErbB receptor familylong-term single-particle trackingoncogenic signalingupconverting nanoparticles

Identifiers

PMID42054992
PMCPMC13195542

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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.