Evidence map›Paper›PMID 21849475›Full record

ArticleMolecular biology of the cell2011

Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin.

Douglas R Boettner, Helena Friesen, Brenda Andrews, Sandra K Lemmon

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Recent insights on gene expression studies onPhysiology and molecular biology of plants : an international journal of functional plant biology · 2022
    Review
  6. Clathrin Light Chains: Not to Be Taken so Lightly.Frontiers in cell and developmental biology · 2021
    Review
  7. Huntingtin-interacting protein family members have a conserved pro-viral function fromProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. TheJournal of cell science · 2019
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Endocytic proteins drive vesicle growth via instability in high membrane tension environment.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

4 authors at 2 institutions in 2 countries.

Douglas R BoettnerDepartment of Molecular and Cellular Pharmacology, University of Miami, Miami, FL 33101, USA.
Helena Friesen
Brenda Andrews
Sandra K Lemmon
University of Miami · USUniversity of Toronto · CA

Funding

Mapping the reference genetic network of a eukaryotic cellR01HG005853 · NHGRI · UNIVERSITY OF TORONTO · PI ANDREWS, BRENDA JEAN, BOONE, CHARLES · 2010 to 2025
$7.6M
SUPPRESSORS OF CLATHRIN DEFICIENCY IN YEASTR01GM055796 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LEMMON, SANDRA K. · 1998 to 2015
$4.7M
Regulation of endoytosis by clathrin light chain.F32GM084677 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BOETTNER, DOUGLAS ROBB · 2008 to 2010
$149k
NHGRI NIH HHS R01 HG005853NHGRI NIH HHS R01-HG005853NIGMS NIH HHS F32 GM084677NIGMS NIH HHS F32-GM084677NIGMS NIH HHS R01 GM055796NIGMS NIH HHS R01-GM055796
6 · The paper itself

Abstract

The role of clathrin light chain (CLC) in clathrin-mediated endocytosis is not completely understood. Previous studies showed that the CLC N-terminus (CLC-NT) binds the Hip1/Hip1R/Sla2 family of membrane/actin-binding factors and that overexpression of the CLC-NT in yeast suppresses endocytic defects of clathrin heavy-chain mutants. To elucidate the mechanistic basis for this suppression, we performed synthetic genetic array analysis with a clathrin CLC-NT deletion mutation (clc1-Δ19-76). clc1-Δ19-76 suppressed the internalization defects of null mutations in three late endocytic factors: amphiphysins (rvs161 and rvs167) and verprolin (vrp1). In actin sedimentation assays, CLC binding to Sla2 inhibited Sla2 interaction with F-actin. Furthermore, clc1-Δ19-76 suppression of the rvs and vrp phenotypes required the Sla2 actin-binding talin-Hip1/R/Sla2 actin-tethering C-terminal homology domain, suggesting that clc1-Δ19-76 promotes internalization by prolonging actin engagement by Sla2. We propose that CLC directs endocytic progression by pruning the Sla2-actin attachments in the clathrin lattice, providing direction for membrane internalization.

Indexed as

Actin CytoskeletonActinsBiological TransportCell MembraneClathrin Light ChainsCytoskeletal ProteinsEndocytosisGene Expression Regulation, FungalMicrofilament ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionActinsClathrin Light ChainsCytoskeletal ProteinsMicrofilament ProteinsRVS161 protein, S cerevisiaeRVS167 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSLA2 protein, S cerevisiaeVRP1 protein, S cerevisiae

Identifiers

PMID21849475
PMCPMC3183023
OpenAlexW1982812269

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.