Evidence map›Paper›PMID 19744925›Full record

ArticleThe Journal of biological chemistry2009

The HECT domain of the ubiquitin ligase Rsp5 contributes to substrate recognition.

Jacqueline R E Lee, Andrea J Oestreich, Johanna A Payne, Mia S Gunawan, Andrew P Norgan, David J Katzmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 25 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 1 institution in 1 country.

Jacqueline R E LeeDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Andrea J Oestreich
Johanna A Payne
Mia S Gunawan
Andrew P Norgan
David J Katzmann
Mayo Clinic · US

Funding

Mechanisms of Endosomal SortingR01GM073024 · NIGMS · MAYO CLINIC ROCHESTER · PI KATZMANN, DAVID J · 2005 to 2013
$2.7M
NIGMS NIH HHS R01 GM073024NIGMS NIH HHS R01 GM73024
6 · The paper itself

Abstract

Ubiquitin modification of endosomal membrane proteins is a signal for active inclusion into the Multivesicular Body (MVB) pathway, resulting in lysosomal degradation. However, the endosome represents a dynamic site of protein sorting with a majority of proteins destined for recycling, rather than MVB targeting. Substrate recognition by ubiquitin ligases is therefore highly regulated. We have investigated substrate recognition by the Nedd4 ortholog Rsp5 as a model for understanding ligase-substrate interactions. Rsp5 interacts directly with its substrate Cps1 via a novel interaction mode. Perturbation of this mode of interaction revealed a compensatory role for the Rsp5 adaptor Bsd2. These results highlight the ability of Rsp5 to interact with substrates via multiple modalities, suggesting additional mechanisms of regulating this interaction and relevant outcomes.

Indexed as

Amino Acid MotifsCarboxypeptidasesEndosomal Sorting Complexes Required for TransportPeptide FragmentsProtein ConformationProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesBSD2 protein, S cerevisiaeCarboxypeptidasesCPS1 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportPeptide FragmentsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase Complexes

Identifiers

PMID19744925
PMCPMC2797283
OpenAlexW2073795788

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.