Flicking the molecular switch underlying MLKL-mediated necroptosis

Joanne M. Hildebrand; Isabelle S. Lucet; James M. Murphy

doi:10.4161/23723556.2014.985550

Flicking the molecular switch underlying MLKL-mediated necroptosis

Joanne M. Hildebrand
, Isabelle S. Lucet
, James M. Murphy

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

4 Citations (Scopus)

Abstract

The pseudokinase domain of the necroptosis effector mixed lineage kinase domain-like (MLKL) functions as a latch to restrain the unleashing of its N-terminal 4-helix bundle (4HB) domain. Cell death mediated by the 4HB domain relies on membrane association and oligomerization, which can be inhibited by an ATP-mimetic small molecule that binds the pseudokinase domain of MLKL.

Original language	English
Article number	e985550
Number of pages	3
Journal	Molecular and Cellular Oncology
Volume	2
Issue number	3
DOIs	https://doi.org/10.4161/23723556.2014.985550
Publication status	Published - 2015
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Access to Document

10.4161/23723556.2014.985550Licence: CC BY-NC

Cite this

@article{b408e7b82d3e407db7896b6987abde6b,

title = "Flicking the molecular switch underlying MLKL-mediated necroptosis",

abstract = "The pseudokinase domain of the necroptosis effector mixed lineage kinase domain-like (MLKL) functions as a latch to restrain the unleashing of its N-terminal 4-helix bundle (4HB) domain. Cell death mediated by the 4HB domain relies on membrane association and oligomerization, which can be inhibited by an ATP-mimetic small molecule that binds the pseudokinase domain of MLKL.",

author = "Hildebrand, \{Joanne M.\} and Lucet, \{Isabelle S.\} and Murphy, \{James M.\}",

note = "Funding Information: This work was supported by a National Health and Medical Research Council fel lowship to JMH, project 1057905 to Publisher Copyright: {\textcopyright} 2015, {\textcopyright} 2015 The Author(s). Published with license by Taylor \& Francis Group, LLC. {\textcopyright} 2015, {\textcopyright} Joanne M Hildebrand, Isabelle S Lucet, and James M Murphy.",

year = "2015",

doi = "10.4161/23723556.2014.985550",

language = "English",

volume = "2",

journal = "Molecular and Cellular Oncology",

issn = "2372-3556",

publisher = "Taylor \& Francis",

number = "3",

}

TY - JOUR

T1 - Flicking the molecular switch underlying MLKL-mediated necroptosis

AU - Hildebrand, Joanne M.

AU - Lucet, Isabelle S.

AU - Murphy, James M.

N1 - Funding Information: This work was supported by a National Health and Medical Research Council fel lowship to JMH, project 1057905 to Publisher Copyright: © 2015, © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC. © 2015, © Joanne M Hildebrand, Isabelle S Lucet, and James M Murphy.

PY - 2015

Y1 - 2015

N2 - The pseudokinase domain of the necroptosis effector mixed lineage kinase domain-like (MLKL) functions as a latch to restrain the unleashing of its N-terminal 4-helix bundle (4HB) domain. Cell death mediated by the 4HB domain relies on membrane association and oligomerization, which can be inhibited by an ATP-mimetic small molecule that binds the pseudokinase domain of MLKL.

AB - The pseudokinase domain of the necroptosis effector mixed lineage kinase domain-like (MLKL) functions as a latch to restrain the unleashing of its N-terminal 4-helix bundle (4HB) domain. Cell death mediated by the 4HB domain relies on membrane association and oligomerization, which can be inhibited by an ATP-mimetic small molecule that binds the pseudokinase domain of MLKL.

UR - https://www.scopus.com/pages/publications/85026342812

U2 - 10.4161/23723556.2014.985550

DO - 10.4161/23723556.2014.985550

M3 - Article

AN - SCOPUS:85026342812

SN - 2372-3556

VL - 2

JO - Molecular and Cellular Oncology

JF - Molecular and Cellular Oncology

IS - 3

M1 - e985550

ER -

Flicking the molecular switch underlying MLKL-mediated necroptosis

Abstract

UN SDGs

Access to Document

Other files and links

Cite this