Evidence map›Paper›PMID 21832070›Full record

ArticleThe Journal of biological chemistry2011

Recycling of the epidermal growth factor receptor is mediated by a novel form of the clathrin adaptor protein Eps15.

Susan Chi, Hong Cao, Yu Wang, Mark A McNiven

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  4. Review
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  12. The Cross-Talk Between EGFR and E-Cadherin.Frontiers in cell and developmental biology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Viral journeys on the intracellular highways.Cellular and molecular life sciences : CMLS · 2018
    Review
  18. Review
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Susan ChiDepartment of Biochemistry and Molecular Biology and Center for Basic Research in Digestive Diseases, Mayo Clinic, Rochester, Minnesota 55905, USA.
Hong Cao
Yu Wang
Mark A McNiven
Mayo Clinic · US

Funding

PILOT AND FEASIBILTY PROGRAMP30DK084567 · NIDDK · MAYO CLINIC ROCHESTER · PI GREGORY J. GORES · 2009 to 2026
$22.2M
CYTOSKELETAL REGULATION OF VESICLE TRANSPORT IN LIVERR01DK044650 · NIDDK · MAYO CLINIC ROCHESTER · PI MC NIVEN, MARK A. · 1997 to 2020
$3.3M
NIDDK NIH HHS P30 DK084567NIDDK NIH HHS P30DK84567NIDDK NIH HHS R01 DK044650NIDDK NIH HHS R01 DK44650
6 · The paper itself

Abstract

Levels of the epidermal growth factor receptor (EGFR) at the cell surface are tightly regulated by a complex endocytic machinery. Following internalization, EGFR is either recycled back to the cell surface or transported to the late endosome/lysosome for degradation. Currently, the molecular machinery that regulates this sorting pathway is only partially defined. Eps15 (EGFR pathway substrate 15) is an endocytic adaptor protein that is well known to support clathrin-mediated internalization of EGFR at the plasma membrane. Using RT-PCR, we have identified a novel short form of Eps15 (Eps15S) from rat liver that lacks the 111 C-terminal amino acids present in the traditional Eps15 form. The goal of this study was to define the functional role of the novel Eps15S form in EGFR trafficking. Overexpression of a mutant form of Eps15S (Eps15S ΔEH2/EH3) did not block EGFR internalization but reduced its recycling to the cell surface. After knockdown of all Eps15 forms, re-expression of Eps15S significantly reduced EGFR degradation while promoting recycling back to the cell surface. In contrast, re-expression of Eps15 did not potentiate receptor recycling. Furthermore, overexpression of the mutant Eps15S substantially reduced cell proliferation, linking EGFR recycling to downstream mitogenic effects. Finally, we found that Eps15S is localized to the Rab11-positive recycling endosome that is disrupted in cells expressing the Eps15S mutant, leading to an accumulation of the EGFR in early endosomes. These findings suggest that distinct forms of Eps15 direct EGFR to either the late endosome/lysosome for degradation (Eps15) or to the recycling endosome for transit back to the cell surface (Eps15S).

Indexed as

Gene Expression RegulationAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBiotinylationCalcium-Binding ProteinsCell Line, TumorClathrinErbB ReceptorsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsLiverMicroscopy, FluorescencePhosphoproteinsProtein BindingAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportCalcium-Binding ProteinsClathrinEPS15 protein, humanEps15 protein, ratErbB ReceptorsIntracellular Signaling Peptides and ProteinsPhosphoproteinsRNA, Small Interfering

Identifiers

PMID21832070
PMCPMC3186422
OpenAlexW2059611728

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.