Evidence map›Paper›PMID 24746795›Full record

ArticleCurrent biology : CB2014

Regulation of clathrin-mediated endocytosis by dynamic ubiquitination and deubiquitination.

Jasper S Weinberg, David G Drubin

Abstract read
In one paragraph

Article in Current biology : CB, 2014. 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
–field-weighted citation impact
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.

  1. Article
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  4. Review
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  11. Article
  12. New insights into the regulation ofFrontiers in neuroscience · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
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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.

Jasper S WeinbergDepartment of Molecular and Cell Biology, 16 Barker Hall, University of California, Berkeley, Berkeley, CA 94720-3202, USA.
David G DrubinDepartment of Molecular and Cell Biology, 16 Barker Hall, University of California, Berkeley, Berkeley, CA 94720-3202, USA. Electronic address: drubin@berkeley.edu.

Funding

Nikon confocal system for improved spatio-dynamic analysis of endocytic trafficking eventsR35GM118149 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DAVID G DRUBIN · 2016 to 2026
$12.0M
The budding yeast endocytic pathwayR01GM050399 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 1997 to 2015
$5.9M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G. · 1989 to 2005
$1.6M
NIGMS NIH HHS R01 GM042759NIGMS NIH HHS R01 GM050399NIGMS NIH HHS R01 GM50399NIGMS NIH HHS R35 GM118149
6 · The paper itself

Abstract

backgroundClathrin-mediated endocytosis in budding yeast requires the regulated recruitment and disassociation of more than 60 proteins at discrete plasma membrane punctae. Posttranslational modifications such as ubiquitination may play important regulatory roles in this highly processive and ordered process. However, although ubiquitination plays an important role in cargo selection, functions for ubiquitination of the endocytic machinery are not known.

resultsWe identified the deubiquitinase (DUB) Ubp7 as a late-arriving endocytic protein. Deletion of the DUBs Ubp2 and Ubp7 resulted in elongation of endocytic coat protein lifetimes at the plasma membrane and recruitment of endocytic proteins to internal membranes. These phenotypes could be replicated by expressing a permanently ubiquitinated version of Ede1, the yeast Eps15 homolog, which is implicated in endocytic site initiation, whereas EDE1 deletion partially suppressed the DUB deletion phenotype. Both DUBs are capable of deubiquitinating Ede1 in vitro.

conclusionsDeubiquitination regulates formation of endocytic sites and stability of the endocytic coat. This regulation appears to occur through Ede1, because permanently ubiquitinated Ede1 phenocopies deletion of UBP2 and UBP7. Moreover, incomplete suppression of the ubp2Δ ubp7Δ phenotype by ede1Δ indicates that ubiquitination and deubiquitination are likely to regulate additional components of the endocytic machinery.

Indexed as

Cell MembraneClathrinEndocytosisEndopeptidasesEndosomal Sorting Complexes Required for TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Specific ProteasesClathrinEde1 protein, S cerevisiaeEndopeptidasesEndosomal Sorting Complexes Required for TransportRSP5 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsubiquitin-Nalpha-protein hydrolaseUbiquitin-Protein Ligase ComplexesUbiquitin-Specific Proteases

Identifiers

PMID24746795
PMCPMC4020423

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Registered trials

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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.