The N terminus of the anti-apoptotic BCL-2 homologue MCL-1 regulates its localization and function. (Q53127485)

11 May 2018

title

The N terminus of the anti-apoptotic BCL-2 homologue MCL-1 regulates its localization and function. (English)

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11 May 2018

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Marc Germain

1

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11 May 2018

Vincent Duronio

series ordinal

2

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11 May 2018

language of work or name

English

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publication date

6 September 2007

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Journal of Biological Chemistry

published in

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volume

282

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issue

44

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page(s)

32233-32242

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Cell death: critical control points

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Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1

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Degradation of Mcl-1 by beta-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization

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Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis.

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Mcl-1 is required for Akata6 B-lymphoma cell survival and is converted to a cell death molecule by efficient caspase-mediated cleavage.

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N-terminal truncation of antiapoptotic MCL1, but not G2/M-induced phosphorylation, is associated with stabilization and abundant expression in tumor cells.

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BH3-ligand regulates access of MCL-1 to its E3 ligase

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Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis

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Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis

21 January 2018

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Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity

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BCL2 family in DNA damage and cell cycle control

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Serine 64 phosphorylation enhances the antiapoptotic function of Mcl-1.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M706408200

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11 May 2018

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11 May 2018