Evidence map›Paper›PMID 28666573›Full record

ArticleImmunity2017

MLKL, the Protein that Mediates Necroptosis, Also Regulates Endosomal Trafficking and Extracellular Vesicle Generation.

Seongmin Yoon, Andrew Kovalenko, Konstantin Bogdanov, David Wallach

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Immunity, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 236 papers.

0numbers the graph read from it
0cells of the map it votes in
236citing papers in PubMed
14.4field-weighted citation impact, top 1% 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

236 citing papers in PubMed, 369 citations in OpenAlex.

  1. Trial
  2. Review
  3. Mechanisms, regulation and clinical relevance of necroptosis.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Review
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  16. Article
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  18. Article
  19. Programmed cell death in osteoarthritis.Apoptosis : an international journal on programmed cell death · 2026
    Review
  20. MLKL/retromer axis controls PD-L1 recycling to compromise antitumor immunity during VCP inhibition-induced necroptosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

176 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Seongmin YoonDepartment of Biomolecular Sciences, The Weizmann Institute of Science, 76100 Rehovot, Israel.
Andrew KovalenkoDepartment of Biomolecular Sciences, The Weizmann Institute of Science, 76100 Rehovot, Israel.
Konstantin BogdanovDepartment of Biomolecular Sciences, The Weizmann Institute of Science, 76100 Rehovot, Israel.
David WallachDepartment of Biomolecular Sciences, The Weizmann Institute of Science, 76100 Rehovot, Israel. Electronic address: d.wallach@weizmann.ac.il.
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of the pseudokinase mixed lineage kinase domain-like (MLKL) upon its phosphorylation by the protein kinase RIPK3 triggers necroptosis, a form of programmed cell death in which rupture of cellular membranes yields release of intracellular components. We report that MLKL also associated with endosomes and controlled the transport of endocytosed proteins, thereby enhancing degradation of receptors and ligands, modulating their induced signaling and facilitating the generation of extracellular vesicles. This role was exerted on two quantitative grades: a constitutive one independent of RIPK3, and an enhanced one, triggered by RIPK3, where the association of MLKL with the endosomes was enhanced, and it was found to bind endosomal sorting complexes required for transport (ESCRT) proteins and the flotillins and to be excluded, together with them, from cells within vesicles. We suggest that release of phosphorylated MLKL within extracellular vesicles serves as a mechanism for self-restricting the necroptotic activity of this protein.

Indexed as

ApoptosisCell LineEndosomesExtracellular VesiclesHumansMutationNecrosisPhosphorylationProtein EngineeringProtein KinasesProtein TransportProteomicsReceptor-Interacting Protein Serine-Threonine KinasesRNA, Small InterferingSignal TransductionMLKL protein, humanProtein KinasesReceptor-Interacting Protein Serine-Threonine KinasesRIPK3 protein, humanRNA, Small InterferingEGFendosomesexosomesextracellular vesiclesinflammationintraluminal vesiclesMLKLmultivesicular bodiesnecroptosisRIPK3TNF

Identifiers

PMID28666573
OpenAlexW2724720631

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.