Evidence map›Paper›PMID 11313482›Full record

ArticleMolecular and cellular biology2001

Localization of the Rsp5p ubiquitin-protein ligase at multiple sites within the endocytic pathway.

G Wang, J M McCaffery, B Wendland, S Dupré, R Haguenauer-Tsapis, J M Huibregtse

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 90 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

G WangSection of Molecular Genetics and Microbiology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712-1095, USA.
J M McCaffery
B Wendland
S Dupré
R Haguenauer-Tsapis
J M Huibregtse
Centre National de la Recherche Scientifique · FRInstitut de Biologie Moléculaire et Cellulaire · FRJohns Hopkins University · US

Funding

MOLECULAR ANALYSIS OF ENDOCYTOSIS PROTEINS IN YEASTR01GM060979 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WENDLAND, BEVERLY R · 2000 to 2013
$4.3M
Specificity of Ubiquitination: the HPVE6/E6AP ParadigmR01CA072943 · NCI · UNIVERSITY OF TEXAS AUSTIN · PI HUIBREGTSE, JON · 1997 to 2011
$3.2M
NCI NIH HHS CA72943NCI NIH HHS R01 CA072943NIGMS NIH HHS GM60979NIGMS NIH HHS R01 GM060979
6 · The paper itself

Abstract

The Saccharomyces cerevisiae RSP5 gene encodes an essential HECT E3 ubiquitin-protein ligase. Rsp5p contains an N-terminal C2 domain, three WW domains in the central portion of the molecule, and a C-terminal catalytic HECT domain. A diverse group of substrates of Rsp5p and vertebrate C2 WW-domain-containing HECT E3s have been identified, including both nuclear and membrane-associated proteins. We determined the intracellular localization of Rsp5p and the determinants necessary for localization, in order to better understand how Rsp5p activities are coordinated. Using both green fluorescent protein fusions to Rsp5p and immunogold electron microscopy, we found that Rsp5p was distributed in a punctate pattern at the plasma membrane, corresponding to membrane invaginations that are likely sites of endosome formation, as well as at perivacuolar sites. The latter appeared to correspond to endocytic intermediates, as these structures were not seen in a sla2/end4-1 mutant, and double-immunogold labeling demonstrated colocalization of Rsp5p with the endosomal markers Pep12p and Vps32p. The C2 domain was an important determinant of localization; however, mutations that disrupted HECT domain function also caused mislocalization of Rsp5p, indicating that enzymatic activity is linked to localization. Deletion of the C2 domain partially stabilized Fur4p, a protein previously shown to undergo Rsp5p- and ubiquitin-mediated endocytosis; however, Fur4p was still ubiquitinated at the plasma membrane when the C2 domain was deleted from the protein. Together, these results indicate that Rsp5p is located at multiple sites within the endocytic pathway and suggest that Rsp5p may function at multiple steps in the ubiquitin-mediated endocytosis pathway.

Indexed as

Saccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesEndocytosisEndosomal Sorting Complexes Required for TransportFungal ProteinsGreen Fluorescent ProteinsImmunohistochemistryLigasesLuminescent ProteinsMutationSaccharomyces cerevisiaeSignal TransductionUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportFungal ProteinsGreen Fluorescent ProteinsLigasesLuminescent ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID11313482
PMCPMC100278
OpenAlexW2164403387

What OpenQuestion holds

Textmetadata
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.