Septins stabilize mitochondria in Tetrahymena thermophila

Eukaryot Cell. 2008 Aug;7(8):1373-86. doi: 10.1128/EC.00085-08. Epub 2008 Jun 27.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / physiology
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / ultrastructure
  • Evolution, Molecular
  • Green Fluorescent Proteins
  • Microscopy, Electron, Transmission
  • Mitochondria / metabolism*
  • Mitochondria / ultrastructure
  • Mitochondrial Membranes / metabolism*
  • Mitochondrial Membranes / ultrastructure
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Tetrahymena thermophila / metabolism*
  • Tetrahymena thermophila / ultrastructure

Substances

  • Cytoskeletal Proteins
  • Protozoan Proteins
  • Green Fluorescent Proteins