Evidence map›Paper›PMID 26246598›Full record

ArticleMolecular biology of the cell2015

Epidermal growth factor-stimulated Akt phosphorylation requires clathrin or ErbB2 but not receptor endocytosis.

Camilo Garay, Gurjeet Judge, Stefanie Lucarelli, Stephen Bautista, Rohan Pandey, Tanveer Singh, Costin N Antonescu

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 107 citations in OpenAlex.

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  9. Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

7 authors at 2 institutions in 2 countries.

Camilo GarayDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada.
Gurjeet JudgeDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada.
Stefanie LucarelliDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada.
Stephen BautistaDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada.
Rohan PandeyDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada.
Tanveer SinghDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada.
Costin N AntonescuDepartment of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada cantonescu@ryerson.ca.
Toronto Metropolitan University · CAUniversity of Geneva · CH

Funding

Canadian Institutes of Health Research 125854
6 · The paper itself

Abstract

Epidermal growth factor (EGF) binding to its receptor (EGFR) activates several signaling intermediates, including Akt, leading to control of cell survival and metabolism. Concomitantly, ligand-bound EGFR is incorporated into clathrin-coated pits--membrane structures containing clathrin and other proteins--eventually leading to receptor internalization. Whether clathrin might regulate EGFR signaling at the plasma membrane before vesicle scission is poorly understood. We compared the effect of clathrin perturbation (preventing formation of, or receptor recruitment to, clathrin structures) to that of dynamin2 (allowing formation of clathrin structures but preventing EGFR internalization) under conditions in which EGFR endocytosis is clathrin dependent. Clathrin perturbation by siRNA gene silencing, with the clathrin inhibitor pitstop2, or knocksideways silencing inhibited EGF-simulated Gab1 and Akt phosphorylation in ARPE-19 cells. In contrast, perturbation of dynamin2 with inhibitors or by siRNA gene silencing did not affect EGF-stimulated Gab1 or Akt phosphorylation. EGF stimulation enriched Gab1 and phospho-Gab1 within clathrin structures. ARPE-19 cells have low ErbB2 expression, and overexpression and knockdown experiments revealed that robust ErbB2 expression bypassed the requirement for clathrin for EGF-stimulated Akt phosphorylation. Thus clathrin scaffolds may represent unique plasma membrane signaling microdomains required for signaling by certain receptors, a function that can be separated from vesicle formation.

Indexed as

Adaptor Proteins, Signal TransducingCell MembraneCells, CulturedClathrinClathrin-Coated VesiclesDynamin IIEndocytosisEpidermal Growth FactorErb-b2 Receptor Tyrosine KinasesHeLa CellsHumansMembrane MicrodomainsPhosphorylationProto-Oncogene Proteins c-aktSignal TransductionSulfonamidesAdaptor Proteins, Signal TransducingClathrinDynamin IIEpidermal Growth FactorERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesGAB1 protein, humanpitstop 2Proto-Oncogene Proteins c-aktSulfonamidesThiazolidines

Identifiers

PMID26246598
PMCPMC4591694
OpenAlexW2191370645

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.