Vimentin intermediate filaments modulate the motility of mitochondria

Oxana E. Nekrasova, Melissa G. Mendez, Ivan S. Chernoivanenko, Pyotr A. Tyurin-Kuzmin, Edward R. Kuczmarski, Vladimir I. Gelfand, Robert D. Goldman, Alexander A. Minin

Research output: Contribution to journalArticle

75 Scopus citations

Abstract

Interactions with vimentin intermediate filaments (VimIFs) affect the motility, distribution, and anchorage of mitochondria. In cells lacking VimIFs or in which VimIF organization is disrupted, the motility of mitochondria is increased relative to control cells that express normal VimIF networks. Expression of wild-type VimIF in vimentin-null cells causes mitochondrial motility to return to normal (slower) rates. In contrast, expressing vimentin with mutations in the mid-region of the N-terminal non-α-helical domain (deletions of residues 41-96 or 45-70, or substitution of Pro-57 with Arg) did not inhibit mitochondrial motility even though these mutants retain their ability to assemble into VimIFs in vivo. It was also found that a vimentin peptide consisting of residues 41-94 localizes to mitochondria. Taken together, these data suggest that VimIFs bind directly or indirectly to mitochondria and anchor them within the cytoplasm.

Original languageEnglish (US)
Pages (from-to)2282-2289
Number of pages8
JournalMolecular biology of the cell
Volume22
Issue number13
DOIs
StatePublished - Jul 1 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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