Evidence map›Paper›PMID 39548957›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2024

Mutations in Mig6 reduce inhibition of the epidermal growth factor receptor.

Samantha Y Hayashi, Steven Pak, Antonio Torlentino, Robert C Rizzo, W Todd Miller

Erratum issuedAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Samantha Y HayashiDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, USA.ORCID https://orcid.org/0000-0003-2885-4078
Steven PakDepartment of Pharmacological Sciences, Stony Brook University, Stony Brook, New York, USA.ORCID https://orcid.org/0000-0002-9493-0983
Antonio TorlentinoDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, USA.ORCID https://orcid.org/0009-0008-2240-8871
Robert C RizzoDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, New York, USA.ORCID https://orcid.org/0000-0003-0525-6147
W Todd MillerDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, USA.ORCID https://orcid.org/0000-0002-6566-0064

Funding

Development, Validation, and Application of Structure-based Tools for Computational Molecular DesignR35GM126906 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI ROBERT C. RIZZO · 2018 to 2026
$3.2M
Chemical Biology Training InterfaceT32GM136572 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI ELIZABETH M BOON, Jessica Chuang Seeliger · 2020 to 2026
$2.9M
Structural and biochemical studies of receptor tyrosine kinasesI01BX006248 · VA · NORTHPORT VA MEDICAL CENTER · PI W Todd MILLER · 2024 to 2026
–
BLRD VA I01 BX006248HHS | National Institutes of Health (NIH) R35GM126906HHS | National Institutes of Health (NIH) T32GM136572NIGMS NIH HHS R35 GM126906NIGMS NIH HHS T32 GM136572U.S. Department of Veterans Affairs (VA) I01BX006248
6 · The paper itself

Abstract

Mitogen-inducible gene 6 (Mig6) is a cellular inhibitor of epidermal growth factor receptor (EGFR) that binds directly to the EGFR kinase domain and interferes with signaling. Reduced Mig6 expression is correlated with increased EGFR activity in multiple cancer models. Here, we investigated whether disease-associated point mutations could reduce the inhibitory potency of Mig6. We show that several cancer-associated mutations, and a mutation derived from Alzheimer's Disease patients, diminish the ability of Mig6 to bind and inhibit EGFR in vitro. In mammalian cells, the mutations decreased the Mig6-induced suppression of basal and EGF-stimulated autophosphorylation, MAP kinase phosphorylation, and cell migration. To probe the mechanisms by which the mutations could lead to reduced Mig6 inhibition, we constructed atomic-level computational models of Mig6 complexed with the EGFR catalytic domain, and performed molecular dynamics simulations for wild-type and mutant complexes.

Indexed as

Adaptor Proteins, Signal TransducingErbB ReceptorsTumor Suppressor ProteinsAlzheimer DiseaseCell MovementHumansMolecular Dynamics SimulationMutationPhosphorylationProtein BindingAdaptor Proteins, Signal TransducingEGFR protein, humanErbB ReceptorsERRFI1 protein, humanTumor Suppressor ProteinsAMBERDOCK6EGFRMig6molecular dynamicsmolecular modelingmutationsnegative regulationper‐residue footprints

Identifiers

PMID39548957
PMCPMC11707679

What OpenQuestion holds

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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.