Document Detail


Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria.
MedLine Citation:
PMID:  21364619     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Autophagy and apoptosis are two important and interconnected stress-response mechanisms. However, the molecular interplay between these two pathways is not fully understood. To study the fate and function of autophagic proteins at the onset of apoptosis, we used a cellular model system in which autophagy precedes apoptosis. IL-3 depletion of Ba/F3 cells caused caspase (casp)-mediated cleavage of Beclin-1 and PI3KC3, two crucial components of the autophagy-inducing complex. We identified two casp cleavage sites in Beclin-1, TDVD(133) and DQLD(149), cleavage at which yields fragments lacking the autophagy-inducing capacity. Noteworthy, the C-terminal fragment, Beclin-1-C, localized predominantly at the mitochondria and sensitized the cells to apoptosis. Moreover, on isolated mitochondria, recombinant Beclin-1-C was able to induce the release of proapoptotic factors. These findings point to a mechanism by which casp-dependent generation of Beclin-1-C creates an amplifying loop enhancing apoptosis upon growth factor withdrawal.
Authors:
E Wirawan; L Vande Walle; K Kersse; S Cornelis; S Claerhout; I Vanoverberghe; R Roelandt; R De Rycke; J Verspurten; W Declercq; P Agostinis; T Vanden Berghe; S Lippens; P Vandenabeele
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell death & disease     Volume:  1     ISSN:  2041-4889     ISO Abbreviation:  Cell Death Dis     Publication Date:  2010  
Date Detail:
Created Date:  2011-03-02     Completed Date:  2011-06-23     Revised Date:  2011-07-26    
Medline Journal Info:
Nlm Unique ID:  101524092     Medline TA:  Cell Death Dis     Country:  England    
Other Details:
Languages:  eng     Pagination:  e18     Citation Subset:  IM    
Affiliation:
VIB, Department for Molecular Biomedical Research, Ghent, Belgium.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Apoptosis*
Apoptosis Regulatory Proteins / analysis,  genetics,  metabolism*
Autophagy*
Caspases / metabolism*
Cell Line
Humans
Interleukin-3 / genetics,  metabolism
Membrane Proteins / analysis,  genetics,  metabolism*
Mice
Mitochondria / metabolism*
Phosphatidylinositol 3-Kinases / genetics,  metabolism
Recombinant Proteins / chemistry,  genetics,  metabolism
Chemical
Reg. No./Substance:
0/Apoptosis Regulatory Proteins; 0/BECN1 protein, human; 0/Becn1 protein, mouse; 0/Interleukin-3; 0/Membrane Proteins; 0/Recombinant Proteins; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC 3.4.22.-/Caspases
Comments/Corrections

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