Evidence map›Paper›PMID 32954645›Full record

ArticleEMBO reports2020

A regulatory region on RIPK2 is required for XIAP binding and NOD signaling activity.

Valentin J Heim, Laura F Dagley, Che A Stafford, Fynn M Hansen, Elise Clayer, Aleksandra Bankovacki, Andrew I Webb, Isabelle S Lucet, John Silke, Ueli Nachbur

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

10 citing papers in PubMed, 13 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

10 authors at 3 institutions in 2 countries.

Valentin J HeimThe Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.
Laura F DagleyThe Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.
Che A StaffordGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Fynn M HansenDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Elise ClayerThe Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.
Aleksandra BankovackiThe Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.
Andrew I WebbThe Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.
Isabelle S LucetThe Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.
John Silke *The Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.ORCID 0000-0002-7611-5774
Ueli Nachbur *The Walter and Eliza Hall Institute of Medical Research, Parkville, Vic., Australia.ORCID 0000-0001-5968-2235
The University of Melbourne · AULudwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DE

Funding

Department of Education and Training | Australian Research Council (ARC) FT130100166Department of Health | National Health and Medical Research Council (NHMRC) 1046986Department of Health | National Health and Medical Research Council (NHMRC) 1057888Department of Health | National Health and Medical Research Council (NHMRC) 1058190Department of Health | National Health and Medical Research Council (NHMRC) 541901Department of Health | National Health and Medical Research Council (NHMRC) 9000220, 1162058EC | Horizon 2020 Framework Programme (H2020) 754388German Excellence Initiative ZUK22
6 · The paper itself

Abstract

Signaling via the intracellular pathogen receptors nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2 requires receptor interacting kinase 2 (RIPK2), an adaptor kinase that can be targeted for the treatment of various inflammatory diseases. However, the molecular mechanisms of how RIPK2 contributes to NOD signaling are not completely understood. We generated FLAG-tagged RIPK2 knock-in mice using CRISPR/Cas9 technology to study NOD signaling mechanisms at the endogenous level. Using cells from these mice, we were able to generate a detailed map of post-translational modifications on RIPK2. Similar to other reports, we did not detect ubiquitination of RIPK2 lysine 209 during NOD2 signaling. However, using site-directed mutagenesis we identified a new regulatory region on RIPK2, which dictates the crucial interaction with the E3 ligase XIAP and downstream signaling outcomes.

Indexed as

Nod2 Signaling Adaptor ProteinReceptor-Interacting Protein Serine-Threonine Kinase 2AnimalsMiceRegulatory Sequences, Nucleic AcidSignal TransductionUbiquitinationNod2 Signaling Adaptor ProteinReceptor-Interacting Protein Serine-Threonine Kinase 2Ripk2 protein, mouseinflammationNOD signalingRIPK2ubiquitinXIAP

Identifiers

PMID32954645
PMCPMC7645253
OpenAlexW3087717211

What OpenQuestion holds

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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.