Evidence map›Paper›PMID 29030480›Full record

ArticleEMBO reports2017

Intersectin-s interaction with DENND2B facilitates recycling of epidermal growth factor receptor.

Maria S Ioannou, Gopinath Kulasekaran, Maryam Fotouhi, Justin J Morein, Chanshuai Han, Sarah Tse, Nadya Nossova, Tony Han, Erin Mannard, Peter S McPherson

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Activation and lineage specific Lag3 expression dynamics in T cells.Journal of immunology (Baltimore, Md. : 1950) · 2026
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  8. The lncRNAOncoTargets and therapy · 2020
    Article
  9. Review
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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 at 1 institution in 1 country.

Maria S IoannouDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada maria.ioannou@mail.mcgill.ca peter.mcpherson@mcgill.ca.ORCID 0000-0001-6252-8626
Gopinath KulasekaranDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Maryam FotouhiDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Justin J MoreinDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Chanshuai HanDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Sarah TseDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Nadya NossovaDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Tony HanDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Erin MannardDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Peter S McPhersonDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada maria.ioannou@mail.mcgill.ca peter.mcpherson@mcgill.ca.ORCID 0000-0001-7806-5662
Montreal Neurological Institute and Hospital · CA

Funding

CIHR FDN‐154305CIHR MOP‐62684
6 · The paper itself

Abstract

Epidermal growth factor (EGF) activates the EGF receptor (EGFR) and stimulates its internalization and trafficking to lysosomes for degradation. However, a percentage of EGFR undergoes ligand-independent endocytosis and is rapidly recycled back to the plasma membrane. Importantly, alterations in EGFR recycling are a common hallmark of cancer, and yet, our understanding of the machineries controlling the fate of endocytosed EGFR is incomplete. Intersectin-s is a multi-domain adaptor protein that is required for internalization of EGFR Here, we discover that intersectin-s binds DENND2B, a guanine nucleotide exchange factor for the exocytic GTPase Rab13, and this interaction promotes recycling of ligand-free EGFR to the cell surface. Intriguingly, upon EGF treatment, DENND2B is phosphorylated by protein kinase D and dissociates from intersectin-s, allowing for receptor targeting to degradation. Our study thus reveals a novel mechanism controlling the fate of internalized EGFR with important implications for cancer.

Indexed as

Signal TransductionAdaptor Proteins, Vesicular TransportCell MembraneEndocytosisEpidermal Growth FactorErbB ReceptorsGuanine Nucleotide Exchange FactorsHEK293 CellsHumansNeoplasmsPhosphorylationProtein BindingProtein Kinase CProtein Transportrab GTP-Binding ProteinsTumor Suppressor ProteinsAdaptor Proteins, Vesicular TransportDENND2D protein, humanEGFR protein, humanEpidermal Growth FactorErbB ReceptorsGuanine Nucleotide Exchange Factorsintersectin 1Protein Kinase Cprotein kinase DRAB13 protein, humanrab GTP-Binding ProteinsTumor Suppressor ProteinsDENN domainendocytosisexocytosisgrowth signallingintersectin‐s

Identifiers

PMID29030480
PMCPMC5709770
OpenAlexW2763808374

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.