MLKL regulates necrotic plasma membrane permeabilization

Lorenzo Galluzzi; Oliver Kepp; Guido Kroemer

doi:10.1038/cr.2014.8

MLKL regulates necrotic plasma membrane permeabilization

Lorenzo Galluzzi
, Oliver Kepp
, Guido Kroemer

Cancer Signaling and Microenvironment (CSM)

Université Paris-Sud
Université Paris Cité
Centre de Recherche des Cordeliers
INSERM; U848
Metabolomics and Cell Biology Platforms
Assistance publique – Hôpitaux de Paris

Research output: Contribution to journal › Article › peer-review

78 Scopus citations

Abstract

Recent data from two independent laboratories have shed new light on the molecular mechanisms by which mixed lineage kinase domain-like (MLKL) promotes a peculiar form of regulated necrosis known as necroptosis. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL appears indeed to form oligomers that localize to the plasma membrane and compromise its ability to preserve ionic homeostasis.

Original language	English
Pages (from-to)	139-140
Number of pages	2
Journal	Cell Research
Volume	24
Issue number	2
DOIs	https://doi.org/10.1038/cr.2014.8
State	Published - Feb 2014

Keywords

Apoptosis
Calcium/metabolism
Cell Membrane Permeability
Cell Membrane/metabolism
HT29 Cells
Humans
Inhibitor of Apoptosis Proteins/metabolism
Necrosis
Phosphorylation
Protein Kinases/metabolism
Protein Serine-Threonine Kinases
Receptor-Interacting Protein Serine-Threonine Kinases/metabolism
Sodium/metabolism
TRPM Cation Channels/metabolism
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/metabolism

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10.1038/cr.2014.8

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title = "MLKL regulates necrotic plasma membrane permeabilization",

abstract = "Recent data from two independent laboratories have shed new light on the molecular mechanisms by which mixed lineage kinase domain-like (MLKL) promotes a peculiar form of regulated necrosis known as necroptosis. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL appears indeed to form oligomers that localize to the plasma membrane and compromise its ability to preserve ionic homeostasis.",

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author = "Lorenzo Galluzzi and Oliver Kepp and Guido Kroemer",

year = "2014",

month = feb,

doi = "10.1038/cr.2014.8",

language = "English",

volume = "24",

pages = "139--140",

journal = "Cell Research",

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T1 - MLKL regulates necrotic plasma membrane permeabilization

AU - Galluzzi, Lorenzo

AU - Kepp, Oliver

AU - Kroemer, Guido

PY - 2014/2

Y1 - 2014/2

N2 - Recent data from two independent laboratories have shed new light on the molecular mechanisms by which mixed lineage kinase domain-like (MLKL) promotes a peculiar form of regulated necrosis known as necroptosis. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL appears indeed to form oligomers that localize to the plasma membrane and compromise its ability to preserve ionic homeostasis.

AB - Recent data from two independent laboratories have shed new light on the molecular mechanisms by which mixed lineage kinase domain-like (MLKL) promotes a peculiar form of regulated necrosis known as necroptosis. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL appears indeed to form oligomers that localize to the plasma membrane and compromise its ability to preserve ionic homeostasis.

KW - Apoptosis

KW - Calcium/metabolism

KW - Cell Membrane Permeability

KW - Cell Membrane/metabolism

KW - HT29 Cells

KW - Humans

KW - Inhibitor of Apoptosis Proteins/metabolism

KW - Necrosis

KW - Phosphorylation

KW - Protein Kinases/metabolism

KW - Protein Serine-Threonine Kinases

KW - Receptor-Interacting Protein Serine-Threonine Kinases/metabolism

KW - Sodium/metabolism

KW - TRPM Cation Channels/metabolism

KW - Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/metabolism

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U2 - 10.1038/cr.2014.8

DO - 10.1038/cr.2014.8

M3 - Article

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AN - SCOPUS:84893728596

SN - 1001-0602

VL - 24

SP - 139

EP - 140

JO - Cell Research

JF - Cell Research

IS - 2

ER -

MLKL regulates necrotic plasma membrane permeabilization

Abstract

Keywords

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