Evidence map›Paper›PMID 20923836›Full record

ArticleJournal of cell science2010

Regulation of Hip1r by epsin controls the temporal and spatial coupling of actin filaments to clathrin-coated pits.

Rebecca J Brady, Cynthia K Damer, John E Heuser, Theresa J O'Halloran

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Cryo-electron tomography pipeline for plasma membranes.bioRxiv : the preprint server for biology · 2024
    Article
  3. Article
  4. Article
  5. The TPLATE complex mediates membrane bending during plant clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
  8. Regulation of the Total Cell Surface Area in DividingFrontiers in cell and developmental biology · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Imaging and modeling the dynamics of clathrin-mediated endocytosis.Cold Spring Harbor perspectives in biology · 2014
    Review
  18. Article
  19. Article
  20. 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

4 authors at 3 institutions in 1 country.

Rebecca J BradyDepartment of Molecular Cell and Developmental Biology, University of Texas at Austin, Austin, TX 78712, USA.
Cynthia K Damer
John E Heuser
Theresa J O'Halloran
The University of Texas at Austin · USCentral Michigan University · USWashington University in St. Louis · US

Funding

INTRACELLULAR ROLE OF CLATHRIN AND ITS REGULATIONR01GM048625 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI O'HALLORAN, THERESA JOYCE · 1994 to 2007
$1.8M
NIGMS NIH HHS R01 GM048625
6 · The paper itself

Abstract

Recently, it has become clear that the actin cytoskeleton is involved in clathrin-mediated endocytosis. During clathrin-mediated endocytosis, clathrin triskelions and adaptor proteins assemble into lattices, forming clathrin-coated pits. These coated pits invaginate and detach from the membrane, a process that requires dynamic actin polymerization. We found an unexpected role for the clathrin adaptor epsin in regulating actin dynamics during this late stage of coated vesicle formation. In Dictyostelium cells, epsin is required for both the membrane recruitment and phosphorylation of the actin- and clathrin-binding protein Hip1r. Epsin-null and Hip1r-null cells exhibit deficiencies in the timing and organization of actin filaments at clathrin-coated pits. Consequently, clathrin structures persist on the membranes of epsin and Hip1r mutants and the internalization of clathrin structures is delayed. We conclude that epsin works with Hip1r to regulate actin dynamics by controlling the spatial and temporal coupling of actin filaments to clathrin-coated pits. Specific residues in the ENTH domain of epsin that are required for the membrane recruitment and phosphorylation of Hip1r are also required for normal actin and clathrin dynamics at the plasma membrane. We propose that epsin promotes the membrane recruitment and phosphorylation of Hip1r, which in turn regulates actin polymerization at clathrin-coated pits.

Indexed as

Receptor Cross-TalkSignal TransductionActin CytoskeletonAdaptor Proteins, Vesicular TransportClathrinCloning, MolecularCoated Pits, Cell-MembraneCytoskeletonDictyosteliumEndocytosisPhosphorylationProtein BindingProtein Interaction Domains and MotifsProtein TransportProtozoan ProteinsAdaptor Proteins, Vesicular TransportClathrinepsinProtozoan Proteins

Identifiers

PMID20923836
PMCPMC2964106
OpenAlexW2114936016

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.