Evidence map›Paper›PMID 22307975›Full record

ArticleEukaryotic cell2012

Bul proteins, a nonredundant, antagonistic family of ubiquitin ligase regulatory proteins.

Tatiana V Novoselova, Kiran Zahira, Ruth-Sarah Rose, James A Sullivan

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
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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

4 authors at 1 institution in 1 country.

Tatiana V NovoselovaSchool of Biological and Chemical Sciences, Queen Mary, University of London, London, United Kingdom.
Kiran Zahira
Ruth-Sarah Rose
James A Sullivan
Queen Mary University of London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G004412/1
6 · The paper itself

Abstract

Like other Nedd4 ligases, Saccharomyces cerevisiae E3 Rsp5p utilizes adaptor proteins to interact with some substrates. Previous studies have indentified Bul1p and Bul2p as adaptor proteins that facilitate the ligase-substrate interaction. Here, we show the identification of a third member of the Bul family, Bul3p, the product of two adjacent open reading frames separated by a stop codon that undergoes readthrough translation. Combinatorial analysis of BUL gene deletions reveals that they regulate some, but not all, of the cellular pathways known to involve Rsp5p. Surprisingly, we find that Bul proteins can act antagonistically to regulate the same ubiquitin-dependent process, and the nature of this antagonistic activity varies between different substrates. We further show, using in vitro ubiquitination assays, that the Bul proteins have different specificities for WW domains and that the two forms of Bul3p interact differently with Rsp5p, potentially leading to alternate functional outcomes. These data introduce a new level of complexity into the regulatory interactions that take place between Rsp5p and its adaptors and substrates and suggest a more critical role for the Bul family of proteins in controlling adaptor-mediated ubiquitination.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid Transport SystemsAmino Acid Transport Systems, BasicCation Transport ProteinsEndosomal Sorting Complexes Required for TransportGene Knockout TechniquesMembrane ProteinsMicrobial ViabilityProtein BindingProtein Interaction Domains and MotifsProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitin-Protein Ligase ComplexesAdaptor Proteins, Signal TransducingAmino Acid Transport SystemsAmino Acid Transport Systems, BasicCAN1 protein, S cerevisiaeCation Transport ProteinsEndosomal Sorting Complexes Required for TransportGAP1 protein, S cerevisiaeMembrane ProteinsRecombinant Fusion ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMF1 protein, S cerevisiaeUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID22307975
PMCPMC3318297
OpenAlexW2095865716

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.