Group of Cell Biology, Institute of Protein Research, Russian Academy of Sciences, Moscow 119988, Russia.
Mol Biol Cell. 2011 Jul 1;22(13):2282-9. doi: 10.1091/mbc.E10-09-0766. Epub 2011 May 11.
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.
与中间丝（VimIFs）相互作用会影响线粒体的运动、分布和锚定。在缺乏 VimIFs 的细胞中，或 VimIF 组织被破坏的细胞中，与表达正常 VimIF 网络的对照细胞相比，线粒体的运动性增加。在 vimentin 缺失的细胞中表达野生型 VimIF 会导致线粒体运动恢复正常（较慢）的速度。相比之下，即使这些突变体保留了在体内组装成 VimIF 的能力，表达在 N 端非α螺旋域的中部有突变的 vimentin（残基 41-96 或 45-70 的缺失，或脯氨酸 57 被精氨酸取代）也不会抑制线粒体的运动性。还发现，由残基 41-94 组成的 vimentin 肽定位于线粒体。总之，这些数据表明 VimIFs 直接或间接地与线粒体结合，并将其锚定在细胞质内。
