Evidence map›Paper›PMID 20493816›Full record

ArticleDevelopmental cell2010

Conformation switching of clathrin light chain regulates clathrin lattice assembly.

Jeremy D Wilbur, Peter K Hwang, Joel A Ybe, Michael Lane, Benjamin D Sellers, Matthew P Jacobson, Robert J Fletterick, Frances M Brodsky

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Clathrin Light Chains: Not to Be Taken so Lightly.Frontiers in cell and developmental biology · 2021
    Review
  11. Article
  12. Clathrin light chain diversity regulates membrane deformation in vitro and synaptic vesicle formation in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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  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

8 authors at 1 institution in 1 country.

Jeremy D WilburGraduate Program in Biophysics, University of California, San Francisco, San Francisco, CA 94143, USA.
Peter K Hwang
Joel A Ybe
Michael Lane
Benjamin D Sellers
Matthew P Jacobson
Robert J Fletterick
Frances M Brodsky
University of California, San Francisco · US

Funding

THE MOLECULAR MECHANISM OF CLATHRIN ASSEMBLYR01GM038093 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BRODSKY, FRANCES M. · 1988 to 2014
$5.0M
A State-of-the-art BIACORE for UCSF Mission BayS10RR023443 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FLETTERICK, ROBERT J · 2007 to 2007
$367k
NCRR NIH HHS S10 RR023443NCRR NIH HHS S10RR023443NIGMS NIH HHS GM038093NIGMS NIH HHS R01 GM038093
6 · The paper itself

Abstract

Clathrin-coated vesicle formation is responsible for membrane traffic to and from the endocytic pathway during receptor-mediated endocytosis and organelle biogenesis, influencing how cells relate to their environment. Generating these vesicles involves self-assembly of clathrin molecules into a latticed coat on membranes that recruits receptors and organizes protein machinery necessary for budding. Here we define a molecular mechanism regulating clathrin lattice formation by obtaining structural information from co-crystals of clathrin subunits. Low resolution X-ray diffraction data (7.9-9.0 A) was analyzed using a combination of molecular replacement with an energy-minimized model and noncrystallographic symmetry averaging. Resulting topological information revealed two conformations of the regulatory clathrin light chain bound to clathrin heavy chain. Based on protein domain positions, mutagenesis, and biochemical assays, we identify an electrostatic interaction between the clathrin subunits that allows the observed conformational variation in clathrin light chains to alter the conformation of the clathrin heavy chain and thereby regulates assembly.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsCattleClathrinClathrin-Coated VesiclesCrystallography, X-RayHumansMacromolecular SubstancesMiceModels, MolecularMolecular Sequence DataOrganellesProtein BindingProtein SubunitsSequence AlignmentClathrinMacromolecular SubstancesProtein Subunits

Identifiers

PMID20493816
PMCPMC2975025
OpenAlexW2086237125

What OpenQuestion holds

Textmetadata
LicenceTDM
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.