Evidence map›Paper›PMID 35238864›Full record

ArticleThe Journal of cell biology2022

Fyn and TOM1L1 are recruited to clathrin-coated pits and regulate Akt signaling.

Rebecca Cabral-Dias, Stefanie Lucarelli, Karolina Zak, Sadia Rahmani, Gurjeet Judge, John Abousawan, Laura F DiGiovanni, Dafne Vural, Karen E Anderson, Michael G Sugiyama and 6 more

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

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  7. Using theBio-protocol · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 6 institutions in 3 countries.

Rebecca Cabral-Dias *Department of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Stefanie Lucarelli *Department of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Karolina ZakDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.ORCID 0000-0001-7266-2204
Sadia RahmaniDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Gurjeet JudgeDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
John AbousawanDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Laura F DiGiovanniDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Dafne VuralDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Karen E AndersonSignalling Programme, Babraham Institute, Babraham Research Campus, Cambridge, UK.ORCID 0000-0002-7394-6660
Michael G SugiyamaDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Gizem GencDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Wanjin HongInstitute of Molecular and Cell Biology, A*STAR, Singapore.
Roberto J BotelhoDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.ORCID 0000-0002-7820-0999
Gregory D FairnDepartment of Pathology, Dalhousie University, Halifax, Nova Scotia, Canada.ORCID 0000-0001-6508-168X
Peter K KimDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0001-6626-0575
Costin N AntonescuDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.ORCID 0000-0001-9192-6340
Toronto Metropolitan University · CAUniversity of Toronto · CAAgency for Science, Technology and Research · SGBabraham Institute · GBDalhousie University · CASt. Michael's Hospital · CA

Funding

Biotechnology and Biological Sciences Research Council BBS/E/B/000C0415CIHR PJT-156355
6 · The paper itself

Abstract

The epidermal growth factor (EGF) receptor (EGFR) controls many aspects of cell physiology. EGF binding to EGFR elicits the membrane recruitment and activation of phosphatidylinositol-3-kinase, leading to Akt phosphorylation and activation. Concomitantly, EGFR is recruited to clathrin-coated pits (CCPs), eventually leading to receptor endocytosis. Previous work uncovered that clathrin, but not receptor endocytosis, is required for EGF-stimulated Akt activation, and that some EGFR signals are enriched in CCPs. Here, we examine how CCPs control EGFR signaling. The signaling adaptor TOM1L1 and the Src-family kinase Fyn are enriched within a subset of CCPs with unique lifetimes and protein composition. Perturbation of TOM1L1 or Fyn impairs EGF-stimulated phosphorylation of Akt2 but not Akt1. EGF stimulation also triggered the TOM1L1- and Fyn-dependent recruitment of the phosphoinositide 5-phosphatase SHIP2 to CCPs. Thus, the recruitment of TOM1L1 and Fyn to a subset of CCPs underlies a role for these structures in the support of EGFR signaling leading to Akt activation.

Indexed as

Adaptor Proteins, Signal TransducingClathrinProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-fynEndocytosisErbB ReceptorsHumansPhosphorylationSignal TransductionAdaptor Proteins, Signal TransducingClathrinErbB ReceptorsFYN protein, humanProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-fynTOM1L1 protein, human

Identifiers

PMID35238864
PMCPMC8899389
OpenAlexW4214860259

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.