Necroptosis: (Last) Message in a Bubble

Peter Vandenabeele; Franck Riquet; Benjamin Cappe

doi:10.1016/j.immuni.2017.07.002

Necroptosis: (Last) Message in a Bubble

Immunity. 2017 Jul 18;47(1):1-3. doi: 10.1016/j.immuni.2017.07.002.

Authors

Peter Vandenabeele¹, Franck Riquet², Benjamin Cappe³

Affiliations

¹ Molecular Signaling and Cell Death Unit, VIB Inflammation Research Center, Ghent, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium; Methusalem Program, Ghent University, Ghent, Belgium. Electronic address: peter.vandenabeele@irc.vib-ugent.be.
² Molecular Signaling and Cell Death Unit, VIB Inflammation Research Center, Ghent, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium; Unité de Glycobiologie Structurale et Fonctionnelle, CNRS-UMR 8576, Université Lille1, Villeneuve d'Ascq, France.
³ Molecular Signaling and Cell Death Unit, VIB Inflammation Research Center, Ghent, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium.

PMID: 28723543
DOI: 10.1016/j.immuni.2017.07.002

Abstract

RIPK3 kinase-mediated phosphorylation of MLKL pseudokinase is the execution event of necroptosis. Two independent reports-in Immunity (Yoon et al., 2017) and Cell (Gong et al., 2017)-reveal that MLKL affects homeostatic membrane trafficking and necroptosis-enhanced bubble formation involving interaction with the ESCRT machinery.

Publication types

Comment

MeSH terms

Animals
Apoptosis*
Cell Membrane / metabolism*
Endosomal Sorting Complexes Required for Transport
Extracellular Vesicles / metabolism*
Humans
Necrosis*
Protein Kinases / immunology
Protein Kinases / metabolism*
Protein Transport*
Receptor-Interacting Protein Serine-Threonine Kinases / metabolism*

Substances

Endosomal Sorting Complexes Required for Transport
MLKL protein, human
Protein Kinases
RIPK3 protein, human
Receptor-Interacting Protein Serine-Threonine Kinases