Evidence map›Paper›PMID 26508657›Full record

ArticleEMBO reports2015

Ubiquitin-Activated Interaction Traps (UBAITs) identify E3 ligase binding partners.

Hazel F O'Connor, Nancy Lyon, Justin W Leung, Poonam Agarwal, Caleb D Swaim, Kyle M Miller, Jon M Huibregtse

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

65 citing papers in PubMed, 90 citations in OpenAlex.

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5 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Hazel F O'ConnorDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
Nancy LyonDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
Justin W LeungDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
Poonam AgarwalDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
Caleb D SwaimDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
Kyle M MillerDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
Jon M HuibregtseDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA huibregtse@austin.utexas.edu.
The University of Texas at Austin · US

Funding

Mechanism and Function of Protein UbiquitinationR01GM103619 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI HUIBREGTSE, JON · 2012 to 2020
$2.5M
NIGMS NIH HHS GM103619NIGMS NIH HHS R01 GM103619
6 · The paper itself

Abstract

We describe a new class of reagents for identifying substrates, adaptors, and regulators of HECT and RING E3s. UBAITs (Ubiquitin-Activated Interaction Traps) are E3-ubiquitin fusion proteins and, in an E1- and E2-dependent manner, the C-terminal ubiquitin moiety forms an amide linkage to proteins that interact with the E3, enabling covalent co-purification of the E3 with partner proteins. We designed UBAITs for both HECT (Rsp5, Itch) and RING (Psh1, RNF126, RNF168) E3s. For HECT E3s, trapping of interacting proteins occurred in vitro either through an E3 thioester-linked lariat intermediate or through an E2 thioester intermediate, and both WT and active-site mutant UBAITs trapped known interacting proteins in yeast and human cells. Yeast Psh1 and human RNF126 and RNF168 UBAITs also trapped known interacting proteins when expressed in cells. Human RNF168 is a key mediator of ubiquitin signaling that promotes DNA double-strand break repair. Using the RNF168 UBAIT, we identify H2AZ--a histone protein involved in DNA repair--as a new target of this E3 ligase. These results demonstrate that UBAITs represent powerful tools for profiling a wide range of ubiquitin ligases.

Indexed as

Amino Acid SequenceBromodomain Containing ProteinsDNA RepairEndosomal Sorting Complexes Required for TransportHistonesHumansMutationPeptide Elongation FactorsProtein BindingProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitin-Conjugating EnzymesBRD2 protein, humanBromodomain Containing ProteinsEndosomal Sorting Complexes Required for TransportHistonesHtz1 protein, S cerevisiaePeptide Elongation FactorsProtein Serine-Threonine KinasesPsh1 protein, S cerevisiaeRecombinant Fusion ProteinsRNF126 protein, humanRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesHECT E3sRING E3sUbiquitinUbiquitin ligases

Identifiers

PMID26508657
PMCPMC4693525
OpenAlexW1859137786

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.