Evidence map›Paper›PMID 38270191›Full record

ArticleMolecular and cellular biology2024

The Deubiquitylase Otub1 Regulates the Chemotactic Response of Splenic B Cells by Modulating the Stability of the γ-Subunit Gng2.

Vincent M Luo, Connie Shen, Samantha Worme, Aanya Bhagrath, Estelle Simo-Cheyou, Steven Findlay, Steven Hébert, William Wai Lam Poon, Zahra Aryanpour, Thomas Zhang and 8 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 99% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

18 authors at 6 institutions in 2 countries.

Vincent M LuoDepartment of Microbiology and Immunology, McGill University, Montréal, Québec, Canada.
Connie ShenDepartment of Microbiology and Immunology, McGill University, Montréal, Québec, Canada.
Samantha WormeLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
Aanya BhagrathMcGill Research Centre for Complex Traits, McGill University, Montréal, Québec, Canada.
Estelle Simo-CheyouDepartment of Microbiology and Immunology, McGill University, Montréal, Québec, Canada.
Steven FindlayLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
Steven HébertLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
William Wai Lam PoonLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
Zahra AryanpourLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
Thomas ZhangLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
René P ZahediManitoba Centre for Proteomics & Systems Biology, University of Manitoba, Winnipeg, Manitoba, Canada.
Jonathan BoulaisInstitut de Recherches Cliniques de Montréal (IRCM), Montreal, Québec, Canada.
Zachary S BuchwaldDepartment of Radiation Oncology, Winship Cancer Institute, Emory University, Atlanta, Georgia, USA.
Christoph H BorchersSegal Cancer Proteomics Centre, Lady Davis Institute for Medical Research, McGill University, Montréal, Québec, Canada.
Jean-Francois CôtéInstitut de Recherches Cliniques de Montréal (IRCM), Montreal, Québec, Canada.
Claudia L KleinmanLady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
Judith N MandlDepartment of Microbiology and Immunology, McGill University, Montréal, Québec, Canada.
Alexandre OrthweinDepartment of Microbiology and Immunology, McGill University, Montréal, Québec, Canada.
McGill University · CAJewish General Hospital · CACancerCare Manitoba · CAEmory University · USMontreal Clinical Research Institute · CAUniversité de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin proteasome system performs the covalent attachment of lysine 48-linked polyubiquitin chains to substrate proteins, thereby targeting them for degradation, while deubiquitylating enzymes (DUBs) reverse this process. This posttranslational modification regulates key features both of innate and adaptative immunity, including antigen presentation, protein homeostasis and signal transduction. Here we show that loss of one of the most highly expressed DUBs, Otub1, results in changes in murine splenic B cell subsets, leading to a significant increase in marginal zone and transitional B cells and a concomitant decrease in follicular B cells. We demonstrate that Otub1 interacts with the γ-subunit of the heterotrimeric G protein, Gng2, and modulates its ubiquitylation status, thereby controlling Gng2 stability. Proximal mapping of Gng2 revealed an enrichment in partners associated with chemokine signaling, actin cytoskeleton and cell migration. In line with these findings, we show that

Indexed as

Chemotaxis, LeukocyteDeubiquitinating EnzymesSpleenUbiquitinAnimalsB-LymphocytesCysteine EndopeptidasesGTP-Binding ProteinsMiceProteasome Endopeptidase ComplexSignal TransductionUbiquitinationCysteine EndopeptidasesDeubiquitinating EnzymesGTP-Binding ProteinsOtub1 protein, mouseProteasome Endopeptidase ComplexUbiquitinB cellchemokine receptorchemotaxisDeubiquitylasedeubiquitylationheterotrimeric G protein gamma subunit 2 (γ-subunit)marginal zonespleen

Identifiers

PMID38270191
PMCPMC10829841
OpenAlexW4391229730

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.