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Rehklau, K.* ; Gurniak, C.B.* ; Conrad, M. ; Friauf, E.* ; Ott, M.* ; Rust, M.B.*

ADF/cofilin proteins translocate to mitochondria during apoptosis but are not generally required for cell death signaling.

Cell Death Differ. 19, 958-967 (2012)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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. Cell Death and Differentiation (2012) 19, 958-967; doi:10.1038/cdd.2011.180; published online 2 December 2011
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Cofilin ; Actin ; Mitochondria ; Apoptosis ; Cytochrome C; ACTIN-DEPOLYMERIZING FACTOR; N-COFILIN; OXIDATIVE STRESS; CYTOSKELETON; PHOSPHORYLATION; MIGRATION; INDUCTION; DYNAMICS; CANCER
ISSN (print) / ISBN 1350-9047
e-ISSN 1476-5403
Quellenangaben Volume: 19, Issue: 6, Pages: 958-967 Article Number: , Supplement: ,
Publisher Nature Publishing Group
Non-patent literature Publications
Reviewing status Peer reviewed