Evidence map›Paper›PMID 31420606›Full record

ArticleOncogene2019

MYO1D binds with kinase domain of the EGFR family to anchor them to plasma membrane before their activation and contributes carcinogenesis.

Yoo-Seung Ko, Jeong A Bae, Keon Young Kim, Sung Jin Kim, Eun Gene Sun, Kyung Hwa Lee, Nacksung Kim, Hyuno Kang, Young-Woo Seo, Hangun Kim and 2 more

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 12% of its field
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

21 citing papers in PubMed, 28 citations in OpenAlex.

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  12. LRRC8A anion channels modulate vascular reactivity via association with myosin phosphatase rho interacting protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 1 country.

Yoo-Seung KoDepartments of Pharmacology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Jeong A BaeDepartments of Pharmacology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Keon Young KimDepartments of Pharmacology, Chonnam National University Medical School, Gwangju, 61469, Korea.ORCID http://orcid.org/0000-0001-9703-9195
Sung Jin KimDepartments of Pharmacology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Eun Gene SunDepartments of Hematology-Oncology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Kyung Hwa LeeDepartments of Pathology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Nacksung KimDepartments of Pharmacology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Hyuno KangKorea Basic Science Institute, Gwangju Center, Gwangju, 61186, Korea.
Young-Woo SeoKorea Basic Science Institute, Gwangju Center, Gwangju, 61186, Korea.
Hangun KimCollege of Pharmacy, Sunchon National University, Sunchon, 57922, North Korea.
Ik Joo ChungDepartments of Hematology-Oncology, Chonnam National University Medical School, Gwangju, 61469, Korea.
Kyung Keun KimDepartments of Pharmacology, Chonnam National University Medical School, Gwangju, 61469, Korea. kimkk@chonnam.ac.kr.
Chonnam National University · KRKorea Basic Science Institute · KRChonnam National University Hospital · KRSunchon National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell surface receptor tyrosine kinase (RTK) exists in a dynamic state, however, it remains unknown how single membrane-spanning RTK proteins are retained in the plasma membrane before their activation. This study was undertaken to investigate how RTK proteins are anchored in the plasma membrane before they bind with their respective extracellular ligands for activation through protein-protein interaction, co-localization, and functional phenotype studies. Here we show that unconventional myosin-I MYO1D functions to hold members of the EGFR family (except ErbB3) at the plasma membrane. MYO1D binds only with unphosphorylated EGFRs and anchors them to underlying actin cytoskeleton at the plasma membrane. The C-terminal end region of the MYO1D tail domain containing a β-meander motif is critical for direct binding with kinase domain of the EGFR family, and expression of the tail domain alone suppresses the oncogenic action of full-length MYO1D. Overexpressed MYO1D increases colorectal and breast cancer cell motility and viability through upregulating EGFR level, and thereby promotes colorectal tumor progression in a syngeneic mouse model. MYO1D is upregulated in human colorectal cancer tissues from advanced stages. Collectively, molecular motor MYO1D plays a distinct role in the dynamic regulation of EGFR family levels by holding them at the plasma membrane before their activation. Overexpressed MYO1D contributes to colorectal carcinogenesis possibly as a novel oncogene and thus may serve as an additional target for suppression of RTK signaling in cancer treatment.

Indexed as

Actin CytoskeletonAnimalsApoptosisCarcinogenesisCell MembraneCell ProliferationColorectal NeoplasmsErbB ReceptorsHumansLigandsMiceMice, Inbred BALB CMice, NudeMyosinsProtein DomainsSignal TransductionEGFR protein, humanErbB ReceptorsLigandsMyo1d protein, mouseMyosins

Identifiers

PMID31420606
OpenAlexW2967965881

What OpenQuestion holds

Textmetadata
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.