Evidence map›Paper›PMID 19798056›Full record

ArticleThe EMBO journal2009

Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor.

Ning Sheng Liu, Li Shen Loo, Eva Loh, Li-Fong Seet, Wanjin Hong

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Plasma Proteomic Profile of Dietary Potassium and Incident CKD.Clinical journal of the American Society of Nephrology : CJASN · 2026
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  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Endocytosis of receptor tyrosine kinases.Cold Spring Harbor perspectives in biology · 2013
    Review
  15. Article
  16. Article
  17. How ubiquitin functions with ESCRTs.Traffic (Copenhagen, Denmark) · 2011
    Review
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Ning Sheng LiuCancer and Developmental Cell Biology Division, Institute of Molecular and Cell Biology, Singapore.
Li Shen Loo
Eva Loh
Li-Fong Seet
Wanjin Hong
Institute of Molecular and Cell Biology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although many proteins have been shown to participate in ligand-stimulated endocytosis of EGF receptor (EGFR), the adaptor protein responsible for interaction of activated EGFR with endocytic machinery remains elusive. We show here that EGF stimulates transient tyrosine phosphorylation of Tom1L1 by the Src family kinases, resulting in transient interaction of Tom1L1 with the activated EGFR bridged by Grb2 and Shc. Cytosolic Tom1L1 is recruited onto the plasma membrane and subsequently redistributes into the early endosome. Mutant forms of Tom1L1 defective in Tyr-phosphorylation or interaction with Grb2 are incapable of interaction with EGFR. These mutants behave as dominant-negative mutants to inhibit endocytosis of EGFR. RNAi-mediated knockdown of Tom1L1 inhibits endocytosis of EGFR. The C-terminal tail of Tom1L1 contains a novel clathrin-interacting motif responsible for interaction with the C-terminal region of clathrin heavy chain, which is important for exogenous Tom1L1 to rescue endocytosis of EGFR in Tom1L1 knocked-down cells. These results suggest that EGF triggers a transient Grb2/Shc-mediated association of EGFR with Tyr-phosphorylated Tom1L1 to engage the endocytic machinery for endocytosis of the ligand-receptor complex.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCells, CulturedEndocytosisEpidermal Growth FactorErbB ReceptorsHeLa CellsHumansMiceModels, BiologicalMutant ProteinsPhosphorylationProtein BindingRNA, Small InterferingTyrosineUp-RegulationAdaptor Proteins, Signal TransducingEpidermal Growth FactorErbB ReceptorsMutant ProteinsRNA, Small InterferingTOM1L1 protein, humanTyrosine

Identifiers

PMID19798056
PMCPMC2756567
OpenAlexW2001960160

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.