Hsp90 modulates the stability of MLKL and is required for TNF-induced necroptosis (Q28603628)

2

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J B Zhao

3

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P P Zhang

4

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Y F Pu

5

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S H Jiang

6

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J J Hou

7

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Y M Cui

8

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X L Jia

9

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S Q Zhang

Creative Commons Attribution 4.0 International

10

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language of work or name

English

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publication date

11 February 2016

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published in

Cell Death and Disease

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volume

7

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issue

2

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page(s)

e2089

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copyright license

start time

1 February 2016

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis

17 March 2017

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The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism

17 March 2017

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Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis

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Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation

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TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90

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Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule

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Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation

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Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

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Heat shock protein 90 inhibitor regulates necroptotic cell death via down-regulation of receptor interacting proteins

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A cytosolic heat shock protein 90 and cochaperone CDC37 complex is required for RIP3 activation during necroptosis

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Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death

29 September 2017

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A plug release mechanism for membrane permeation by MLKL.

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MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates.

29 September 2017

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Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3.

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A central role for the Hsp90.Cdc37 molecular chaperone module in interleukin-1 receptor-associated-kinase-dependent signaling by toll-like receptors.

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Requirement of Hsp90 activity for IkappaB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-kappaB activation.

29 September 2017

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29 September 2017

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Heat-shock protein hsp90 governs the activity of pp60v-src kinase

29 September 2017

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Geldanamycin-induced destabilization of Raf-1 involves the proteasome

29 September 2017

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Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association

3 June 2018

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The native v-Raf.hsp90.p50 heterocomplex contains a novel immunophilin of the FK506 binding class

3 June 2018

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Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis

3 June 2018

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Crossref

https://api.crossref.org/works/10.1038%2FCDDIS.2015.390

21 January 2018

Identifiers

DOI

10.1038/CDDIS.2015.390

1 reference

Dimensions Publication ID

1040002239

0 references

1 reference

1 reference

PubMed publication ID

26866270

1 reference