Evidence map›Paper›PMID 22323290›Full record

ArticleMolecular biology of the cell2012

FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis.

Erin E Mulkearns, Jonathan A Cooper

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice.Frontiers in cell and developmental biology · 2016
    Review
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

2 authors at 2 institutions in 1 country.

Erin E MulkearnsMolecular and Cellular Biology Program, University of Washington, Seattle, WA 98195, USA.
Jonathan A Cooper
Fred Hutch Cancer Center · USUniversity of Washington · US

Funding

Translational Bioimaging Core Shared ResourceP30CA015704 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Thomas James Lynch · 1985 to 2026
$296.4M
In vivo functions of possible tumor suppressor Dab2R01GM066257 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI COOPER, JONATHAN A · 2003 to 2011
$3.3M
VIRAL ONCOLOGYT32CA009229 · NCI · UNIVERSITY OF WASHINGTON · PI LINIAL, MAXINE L · 1985 to 2007
$3.0M
NCI NIH HHS P30 CA015704NCI NIH HHS T32 CA009229NIGMS NIH HHS R01 GM066257NIGMS NIH HHS R01-GM66257
6 · The paper itself

Abstract

Clathrin-mediated endocytosis regulates the internalization of many nutrient and signaling receptors. Clathrin and endocytic accessory proteins are recruited to receptors by specific adaptors. The adaptor Disabled-2 (Dab2) recruits its cargoes, including the low-density lipoprotein receptor (LDLR), and mediates endocytosis, even when the major adaptor protein AP2 is depleted. We hypothesized that the accessory proteins normally recruited by AP2 may be recruited by Dab2 if AP2 is absent. We identified one such accessory protein, the F-BAR protein FCH domain only-2 (FCHO2), as a major Dab2-interacting protein. The μ-homology domain (μHD) of FCHO2 binds directly to DPF sequences in Dab2 that also bind AP2. Disrupting the Dab2-FCHO2 interaction inhibited Dab2-mediated LDLR endocytosis in AP2-depleted cells. Depleting FCHO2 reduced the number but increased the size of clathrin structures on the adherent surface of HeLa cells and inhibited LDLR and transferrin receptor clustering. However, LDLR was internalized efficiently by FCHO2-deficient cells when additional time was provided for LDLR to enter the enlarged structures before budding, suggesting that later steps of endocytosis are normal under these conditions. These results indicate FCHO2 regulates the size of clathrin structures, and its interaction with Dab2 is needed for LDLR endocytosis under conditions of low AP2.

Indexed as

Adaptor Protein Complex 2Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBase SequenceCell LineClathrin-Coated VesiclesEndocytosisFatty Acid-Binding ProteinsHeLa CellsHumansMembrane ProteinsMutagenesis, Site-DirectedMutant ProteinsProtein Interaction Domains and MotifsProteinsReceptors, LDLAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsDAB2 protein, humanFatty Acid-Binding ProteinsFCHO2 protein, humanMembrane ProteinsMutant ProteinsProteinsReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsRNA, Small InterferingTumor Suppressor Proteins

Identifiers

PMID22323290
PMCPMC3315808
OpenAlexW2037403702

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.