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Cited by 279

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

Role of JNK1-dependent Bcl-2 Phosphorylation in Ceramide-induced Macroautophagy

Open access
Pattingre, Sophie, Bauvy, Chantal, Carpentier, Stéphane, Levade, Thierry, Levine, Beth, Codogno, Patrice·2009·Journal of Biological Chemistry

Abstract

Macroautophagy is a vacuolar lysosomal catabolic pathway that is stimulated during periods of nutrient starvation to preserve cell integrity. Ceramide is a bioactive sphingolipid associated with a large range of cell processes. Here we show that short-chain ceramides (C(2)-ceramide and C(6)-ceramide) and stimulation of the de novo ceramide synthesis by tamoxifen induce the dissociation of the complex formed between the autophagy protein Beclin 1 and the anti-apoptotic protein Bcl-2. This dissociation is required for macroautophagy to be induced either in response to ceramide or to starvation. Three potential phosphorylation sites, Thr(69), Ser(70), and Ser(87), located in the non-structural N-terminal loop of Bcl-2, play major roles in the dissociation of Bcl-2 from Beclin 1. We further show that activation of c-Jun N-terminal protein kinase 1 by ceramide is required both to phosphorylate Bcl-2 and to stimulate macroautophagy. These findings reveal a new aspect of sphingolipid signaling in up-regulating a major cell process involved in cell adaptation to stress.

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Crossref · 10.1074/jbc.m805920200

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Cited by

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Metadata

Authors
Pattingre, S., Bauvy, C., Carpentier, S., Levade, T., Levine, B., & Codogno, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2009-01
Volume
284
Issue
5
Pages
2719-2728
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2001284886
Cited by
279
References
13
FWCI
14.67
Type
journal article
Language
en
Open access
hybrid

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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