Evidence map›Paper›PMID 26303906›Full record

ArticleThe EMBO journal2015

RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.

Nava Zaarur, Xiaobin Xu, Patrick Lestienne, Anatoli B Meriin, Mark McComb, Catherine E Costello, Gary P Newnam, Rakhee Ganti, Nina V Romanova, Maruda Shanmugasundaram and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 61 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

17 authors at 8 institutions in 4 countries.

Nava ZaarurDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Xiaobin XuCenter for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Patrick LestienneINSERM U 1053, University of Bordeaux Segalen, Bordeaux, France.
Anatoli B MeriinDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Mark McCombCenter for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Catherine E CostelloDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Gary P NewnamSchool of Biology, Georgia Institute of Technology, Atlanta, GA, USA.
Rakhee GantiSchool of Biology, Georgia Institute of Technology, Atlanta, GA, USA.
Nina V RomanovaLaboratory of Amyloid Biology and Institute of Translational Biomedicine, St. Petersburg State University, St. Petersburg, Russia.
Maruda ShanmugasundaramDepartment of Chemistry, University at Albany, State University of New York, Albany, NY, USA.
Sara T N SilvaInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
Tiago M BandeirasInstituto de Biologia Experimental e Tecnológica, Oeiras, Portugal.
Pedro M MatiasInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal Instituto de Biologia Experimental e Tecnológica, Oeiras, Portugal.
Kirill S LobachevSchool of Biology, Georgia Institute of Technology, Atlanta, GA, USA.
Igor K LednevDepartment of Chemistry, University at Albany, State University of New York, Albany, NY, USA.
Yury O ChernoffSchool of Biology, Georgia Institute of Technology, Atlanta, GA, USA Laboratory of Amyloid Biology and Institute of Translational Biomedicine, St. Petersburg State University, St. Petersburg, Russia yury.chernoff@biology.gatech.edu sherma1@bu.edu.
Michael Y ShermanDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA yury.chernoff@biology.gatech.edu sherma1@bu.edu.
Boston University · USGeorgia Institute of Technology · USInstituto de Biologia Experimental e Tecnológica · PTSt Petersburg University · RUAlbany State University · USInserm · FRUniversidade Nova de Lisboa · PTUniversity at Albany, State University of New York · US

Funding

Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Cellular Mechanisms of Aggregation of Abnormal ProteinsR01GM086890 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SHERMAN, MICHAEL Y · 2009 to 2012
$1.5M
Ubiquitin and regulation of prion induction by a short-lived proteinR01GM093294 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2011 to 2014
$1.3M
NHLBI NIH HHS HHSN268201000031CNIGMS NIH HHS P41 GM104603NIGMS NIH HHS R01 GM086890NIGMS NIH HHS R01GM086890NIGMS NIH HHS R01 GM093294NIGMS NIH HHS R01GM093294PHS HHS HHSN268201000031C
6 · The paper itself

Abstract

The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome-like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin-1 interacted directly with the RuvbL1 barrel-like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation.

Indexed as

AmyloidATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesHeat-Shock ProteinsHEK293 CellsHeLa CellsHumansNerve Tissue ProteinsOrganellesAmyloidATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesHeat-Shock ProteinsNerve Tissue ProteinsRUVBL1 protein, humanRUVBL2 protein, humanSNCAIP protein, humanaggresomeamyloiddisaggregationRuvbL

Identifiers

PMID26303906
PMCPMC4570522
OpenAlexW2118442571

What OpenQuestion holds

Textmetadata
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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.