Evidence map›Paper›PMID 26042225›Full record

ReviewFrontiers in molecular biosciences2015

The role of molecular chaperones in clathrin mediated vesicular trafficking.

Rui Sousa, Eileen M Lafer

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
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  14. Article
  15. The Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2019
    Review
  16. Review
  17. From Pathogenesis to Novel Therapeutics for Spinocerebellar Ataxia Type 3: Evading Potholes on the Way to Translation.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2019
    Review
  18. Modulation of Amyloid States by Molecular Chaperones.Cold Spring Harbor perspectives in biology · 2019
    Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Rui SousaDepartment of Biochemistry and Center for Biomedical Neuroscience, University of Texas Health Science Center at San Antonio San Antonio, TX, USA.
Eileen M LaferDepartment of Biochemistry and Center for Biomedical Neuroscience, University of Texas Health Science Center at San Antonio San Antonio, TX, USA.
The University of Texas Health Science Center at San Antonio · US

Funding

MOLECULAR BIOLOGY OF THE SYNAPSER01NS029051 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LAFER, EILEEN M. · 1990 to 2012
$4.0M
Molecular Biology of the SynapseR56NS029051 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LAFER, EILEEN M. · 2008 to 2013
$744k
NINDS NIH HHS R01 NS029051NINDS NIH HHS R56 NS029051
6 · The paper itself

Abstract

The discovery that the 70 kD "uncoating ATPase," which removes clathrin coats from vesicles after endocytosis, is the constitutively expressed Hsc70 chaperone was a surprise. Subsequent work, however, revealed that uncoating is an archetypal Hsp70 reaction: the cochaperone auxilin, which contains a clathrin binding domain and an Hsc70 binding J domain, recruits Hsc70(*)ATP to the coat and, concomitant with ATP hydrolysis, transfers it to a hydrophobic Hsc70-binding element found on a flexible tail at the C-terminus of the clathrin heavy chain. Release of clathrin in association with Hsc70(*)ADP follows, and the subsequent, persistent association of clathrin with Hsc70 is important to prevent aberrant clathrin polymerization. Thus, the two canonical functions of Hsp70-dissociation of existing protein complexes or aggregates, and binding to a protein to inhibit its inappropriate aggregation-are recapitulated in uncoating. Association of clathrin with Hsc70 in vivo is regulated by Hsp110, an Hsp70 NEF that is itself a member of the Hsp70 family. How Hsp110 activity is itself regulated to make Hsc70-free clathrin available for endocytosis is unclear, though at synapses it's possible that the influx of calcium that accompanies depolarization activates the Ca(++)/calmodulin dependent calcineurin phosphatase which then dephosphorylates and activates Hsp110 to stimulate ADP/ATP exchange and release clathrin from Hsc70(*)ADP:clathrin complexes.

Indexed as

auxilinchaperoneclathrinendocytosisHsc70Hsp110Hsp70NEF

Identifiers

PMID26042225
PMCPMC4436892
OpenAlexW1546638544

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.