Evidence map›Paper›PMID 33956941›Full record

ArticleThe Journal of cell biology2021

MyD88 oligomer size functions as a physical threshold to trigger IL1R Myddosome signaling.

Rafael Deliz-Aguirre, Fakun Cao, Fenja H U Gerpott, Nichanok Auevechanichkul, Mariam Chupanova, YeVin Mun, Elke Ziska, Marcus J Taylor

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-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

32 citing papers in PubMed, 50 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

8 authors at 1 institution in 1 country.

Rafael Deliz-Aguirre *Max Planck Institute for Infection Biology, Berlin, Germany.ORCID 0000-0002-1861-8808
Fakun Cao *Max Planck Institute for Infection Biology, Berlin, Germany.ORCID 0000-0003-0542-4374
Fenja H U GerpottMax Planck Institute for Infection Biology, Berlin, Germany.ORCID 0000-0002-1728-3049
Nichanok AuevechanichkulMax Planck Institute for Infection Biology, Berlin, Germany.
Mariam ChupanovaMax Planck Institute for Infection Biology, Berlin, Germany.
YeVin MunMax Planck Institute for Infection Biology, Berlin, Germany.ORCID 0000-0002-2928-6466
Elke ZiskaMax Planck Institute for Infection Biology, Berlin, Germany.ORCID 0000-0002-4119-3916
Marcus J TaylorMax Planck Institute for Infection Biology, Berlin, Germany.ORCID 0000-0002-0904-2122
Max Planck Institute for Infection Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A recurring feature of innate immune receptor signaling is the self-assembly of signaling proteins into oligomeric complexes. The Myddosome is an oligomeric complex that is required to transmit inflammatory signals from TLR/IL1Rs and consists of MyD88 and IRAK family kinases. However, the molecular basis for how Myddosome proteins self-assemble and regulate intracellular signaling remains poorly understood. Here, we developed a novel assay to analyze the spatiotemporal dynamics of IL1R and Myddosome signaling in live cells. We found that MyD88 oligomerization is inducible and initially reversible. Moreover, the formation of larger, stable oligomers consisting of more than four MyD88s triggers the sequential recruitment of IRAK4 and IRAK1. Notably, genetic knockout of IRAK4 enhanced MyD88 oligomerization, indicating that IRAK4 controls MyD88 oligomer size and growth. MyD88 oligomer size thus functions as a physical threshold to trigger downstream signaling. These results provide a mechanistic basis for how protein oligomerization might function in cell signaling pathways.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsHumansImmunity, InnateInterleukin-1 Receptor-Associated KinasesMiceMyeloid Differentiation Factor 88Protein MultimerizationReceptors, Interleukin-1 Type ISignal TransductionAdaptor Proteins, Signal TransducingIL1R1 protein, mouseInterleukin-1 Receptor-Associated KinasesIrak1 protein, mouseIrak4 protein, mouseMyeloid Differentiation Factor 88Receptors, Interleukin-1 Type I

Identifiers

PMID33956941
PMCPMC8105725
OpenAlexW3159653851

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.