Document Detail

ADF/cofilin proteins translocate to mitochondria during apoptosis but are not generally required for cell death signaling.
MedLine Citation:
PMID:  22139132     Owner:  NLM     Status:  MEDLINE    
Non-muscle cofilin (n-cofilin) is a member of the ADF/cofilin family of actin depolymerizing proteins. Recent studies reported a mitochondrial translocation of n-cofilin during apoptosis. As these studies also revealed impaired cytochrome c release and a block in apoptosis upon small interfering RNA-mediated n-cofilin knockdown, n-cofilin was postulated to be essential for apoptosis induction. To elucidate the general importance of ADF/cofilin activity for apoptosis, we exposed mouse embryonic fibroblasts deficient for n-cofilin, ADF (actin depolymerizing factor), or all ADF/cofilin isoforms to well-characterized apoptosis inducers. Cytochrome c release, caspase-3 activation, and apoptotic chromatin condensation were unchanged in all mutant fibroblasts. Thus, we conclude that ADF/cofilin activity is not generally required for induction or progression of apoptosis in mammalian cells. Interestingly, mitochondrial association of ADF and n-cofilin during apoptosis was preceded by, and dependent on, actin that translocated by a yet unknown mechanism to mitochondria during cell death.
K Rehklau; C B Gurniak; M Conrad; E Friauf; M Ott; M B Rust
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-12-02
Journal Detail:
Title:  Cell death and differentiation     Volume:  19     ISSN:  1476-5403     ISO Abbreviation:  Cell Death Differ.     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-05-07     Completed Date:  2012-09-10     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  9437445     Medline TA:  Cell Death Differ     Country:  England    
Other Details:
Languages:  eng     Pagination:  958-67     Citation Subset:  IM    
Neurobiology/Neurophysiology Group, Department of Biology, University of Kaiserslautern, Kaiserslautern, Germany.
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MeSH Terms
Actins / metabolism
Caspase 3 / metabolism
Cells, Cultured
Cofilin 1 / antagonists & inhibitors,  genetics,  metabolism*
Cytochromes c / metabolism
Destrin / antagonists & inhibitors,  genetics,  metabolism*
Fibroblasts / drug effects,  metabolism
Hydrogen Peroxide / toxicity
Mitochondria / metabolism*
RNA Interference
RNA, Small Interfering / metabolism
Staurosporine / pharmacology
Reg. No./Substance:
0/Actins; 0/Cofilin 1; 0/Destrin; 0/RNA, Small Interfering; 62996-74-1/Staurosporine; 7722-84-1/Hydrogen Peroxide; 9007-43-6/Cytochromes c; EC 3.4.22.-/Caspase 3

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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