Evidence map›Paper›PMID 11157986›Full record

ArticleThe Journal of cell biology2001

Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo.

S L Newmyer, S L Schmid

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 150 citations in OpenAlex.

  1. Article
  2. Mitochondrial ROS control neuronal excitability and cell fate in frontotemporal dementia.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Allosteric heat shock protein 70 inhibitors block hepatitis C virus assembly.International journal of antimicrobial agents · 2016
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

S L NewmyerDepartment of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
S L Schmid
Scripps Research Institute · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
THE CLATHRIN COATED VESICLE CYCLER37MH061345 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHMID, SANDRA L. · 2000 to 2009
$4.7M
NCI NIH HHS CA58689NIMH NIH HHS R37 MH061345NIMH NIH HHS R37-MH61345
6 · The paper itself

Abstract

Within the clathrin-coated vesicle (CCV) cycle, coat assembly drives the internalization of receptors from the cell surface and disassembly allows for the processing of internalized ligands. The heat shock cognate protein, hsc70, has been implicated in regulating coat disassembly. We find that in cells overexpressing ATPase-deficient hsc70 mutants, uncoating of CCVs is inhibited in vivo, and the majority of unassembled cytosolic clathrin shifts to an assembled pool that cofractionates with AP1 and AP2. Surprisingly, this assembled pool of coat proteins accumulates in the absence of cargo receptors, suggesting that disruption of hsc70 activity may cause misassembly of empty clathrin cages. The strongest effect of overexpression of hsc70 mutants is a block in transferrin receptor (TfnR) recycling, which cannot be accounted for by the degree of inhibition of uncoating of endocytic CCVs. These results suggest that hsc70 participates in multiple transport and/or sorting events between endosomal compartments. Additionally, the mutant-expressing cells are defective at internalizing transferrin. In the most potent case, the initial rate of uptake is inhibited 10-fold, and TfnR levels double at the cell surface. Our findings demonstrate that hsc70 indeed regulates coat disassembly and also suggest that this chaperone broadly modulates clathrin dynamics throughout the CCV cycle.

Indexed as

Adenosine TriphosphatasesAdenoviridaeCell FractionationClathrinClathrin-Coated VesiclesElectrophoresis, Polyacrylamide GelEndocytosisHeLa CellsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansImmunoblottingKineticsMicroscopy, ConfocalModels, BiologicalMutationAdenosine TriphosphatasesClathrinHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA8 protein, humanReceptors, Transferrin

Identifiers

PMID11157986
PMCPMC2196005
OpenAlexW2020419088

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.