Evidence map›Paper›PMID 26711259›Full record

ArticleMolecular and cellular biology2015

Negative Regulation of CARD11 Signaling and Lymphoma Cell Survival by the E3 Ubiquitin Ligase RNF181.

Sarah M Pedersen, Waipan Chan, Rakhi P Jattani, deMauri S Mackie, Joel L Pomerantz

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

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  16. The E3 Ubiquitin Ligase RNF7 Negatively Regulates CARD14/CARMA2sh Signaling.International journal of molecular sciences · 2017
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Sarah M PedersenDepartment of Biological Chemistry and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Waipan ChanDepartment of Biological Chemistry and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Rakhi P JattaniDepartment of Biological Chemistry and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
deMauri S MackieDepartment of Biological Chemistry and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Joel L PomerantzDepartment of Biological Chemistry and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA joel.pomerantz@jhmi.edu.ORCID http://orcid.org/0000-0002-5030-1018
Johns Hopkins University · US

Funding

Training Program in Cellular and Molecular MedicineT32GM008752 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI RAO, RAJINI · 2000 to 2019
$11.7M
Regulation of CARD11 signaling in normal and dysregulated lymphocyte developmentR01CA177600 · NCI · JOHNS HOPKINS UNIVERSITY · PI POMERANTZ, JOEL L · 2013 to 2017
$1.7M
Isolation of Regulators of Immune Cell BehaviorR21AI118606 · NIAID · JOHNS HOPKINS UNIVERSITY · PI POMERANTZ, JOEL L · 2015 to 2016
$446k
Identifying Regulators of Oncogenic CARD11 in Diffuse Large B Cell LymphomaF31CA171532 · NCI · JOHNS HOPKINS UNIVERSITY · PI MACKIE, DEMAURI · 2013 to 2015
$128k
NCI NIH HHS F31 CA171532NCI NIH HHS F31CA171532NCI NIH HHS R01 CA177600NCI NIH HHS R01CA177600NIAID NIH HHS R21 AI118606NIAID NIH HHS R21AI118606NIGMS NIH HHS T32 GM008752
6 · The paper itself

Abstract

NF-κB activation downstream of antigen receptor engagement is a highly regulated event required for lymphocyte activation during the adaptive immune response. The pathway is often dysregulated in lymphoma, leading to constitutive NF-κB activity that supports the aberrant proliferation of transformed lymphocytes. To identify novel regulators of antigen receptor signaling to NF-κB, we developed bioluminescence resonance energy transfer-based interaction cloning (BRIC), a screening strategy that can detect protein-protein interactions in live mammalian cells in a high-throughput manner. Using this strategy, we identified the RING finger protein RNF181 as an interactor of CARD11, a key signaling scaffold in the antigen receptor pathway. We present evidence that RNF181 functions as an E3 ubiquitin ligase to inhibit antigen receptor signaling to NF-κB downstream of CARD11. The levels of the obligate signaling protein Bcl10 are reduced by RNF181 even prior to signaling, and Bcl10 can serve as a substrate for RNF181 E3 ligase activity in vitro. Furthermore, RNF181 limits the proliferation of human diffuse large B cell lymphoma cells that depend upon aberrant CARD11 signaling to NF-κB for growth and survival in culture. Our results define a new regulatory checkpoint that can modulate the output of CARD11 signaling to NF-κB in both normal and transformed lymphocytes.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingB-Cell CLL-Lymphoma 10 ProteinCARD Signaling Adaptor ProteinsCell SurvivalGuanylate CyclaseHEK293 CellsHumansJurkat CellsLymphomaNF-kappa BProtein Interaction MapsProtein Structure, TertiaryReceptors, AntigenUbiquitinationUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingB-Cell CLL-Lymphoma 10 ProteinBCL10 protein, humanCARD11 protein, humanCARD Signaling Adaptor ProteinsGuanylate CyclaseNF-kappa BReceptors, AntigenRNF181 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID26711259
PMCPMC4760215
OpenAlexW2202564443

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.