Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1793, Issue 12, Pages 1876-1885Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2009.10.011
Keywords
Apoptosis; NOA36; ZNF330; Etoposide; Camptothecin; Mitochondria
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Funding
- 'Ministerio de Ciencia y Tecnologia' of Spain [SAF2003-06398]
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Translocations of regulator proteins from or to the mitochondria are key events in apoptosis regulation. NOA36/ZNF330 is a highly evolutionary conserved protein with a characteristic cystein-rich domain. In this work we address its mitochondrial localization and we demonstrate that a blockage of endogenous NOA36/ZNF330 expression by small-interfering RNA (siRNA) reduced apoptotic response to etoposide (ETO), camptothecin (CPT) and staurosporine (STS) but not to CH 11 anti-Fas antibody or tumour-necrosis-factor-related apoptosis-inducing ligand (TRAIL) in HeLa cells. In contrast, when ectopically expressed in the cytoplasm, NOA36/ZNF330 induces apoptotic cell death. We also found that the domain responsible for this proapoptotic activity is located its cystein-rich region. We propose that NOA36/ZNF330 is translocated from the mitochondria, to the cytoplasm when apoptosis is induced and that it contributes to cytochrome c release. (C) 2009 Elsevier B.V. All rights reserved.
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