Eukaryotic Cell · 2008 · 47 citations · 66 references
Life SciencesBiologyCell BiologyApoptosisAutophagyMitochondrial BiologyMitochondrial FunctionMitochondrial MembranesMitochondrial PhysiologyMitochondrial StructureMitochondrial UltrastructureOrganelle PhysiologyApoptotic MorphologyGreen Fluorescent Protein ReportersMitochondria-associated MembranesMitochondrial Intermembrane Space ProteinsNuclear Envelope Proteins
We describe phylogenetic and functional studies of three septins in the free-living ciliate Tetrahymena thermophila. Both deletion and overproduction of septins led to vacuolization of mitochondria, destabilization of the nuclear envelope, and increased autophagy. All three green fluorescent protein-tagged septins localized to mitochondria. Specific septins localized to the outer mitochondrial membrane, to septa formed during mitochondrial scission, or to the mitochondrion-associated endoplasmic reticulum. The only other septins known to localize to mitochondria are human ARTS and murine M-septin, both alternatively spliced forms of Sep4 (S. Larisch, Cell Cycle 3:1021-1023, 2004; S. Takahashi, R. Inatome, H. Yamamura, and S. Yanagi, Genes Cells 8:81-93, 2003). It therefore appears that septins have been recruited to mitochondrial functions independently in at least two eukaryotic lineages and in both cases are involved in apoptotic events.
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Molecular characterization of mitochondrial apoptosis-inducing factor
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Predicting Coiled Coils from Protein Sequences
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