Vimentin intermediate filaments modulate the motility of mitochondria

Abstract

The vimentin N-terminal domain contains the sequence responsible for the interaction with mitochondria. The interaction of vimentin intermediate filaments with mitochondria causes the inhibition of their movements and contributes to their anchoring in cytoplasm.

Giant axonal neuropathy–associated gigaxonin mutations impair intermediate filament protein degradation

“…In support of defective transport mechanisms, we found accumulation of mitochondria in close proximity to and within the IF aggregates. This most likely reflects the previously reported interactions, binding, and anchorage of mitochondria to both VIFs (45) and NF IFs (46). It is also important to note that the nervous system contains both neuronal and glial cells.…”

Molecular Mechanisms and Physiological Significance of Organelle Interactions and Cooperation

“…Therefore, CluA is most likely not an adaptor protein linking mitochondria to the cytoskeleton. Instead we suggest that D. discoideum must have a novel adaptor protein not yet identified; perhaps an intermediate filament as indicated in 3T3 fibroblast cells (Nekrasova et al, 2011).…”

“…Drosophila mitochondria primarily use microtubules (Cox and Spradling, 2009), as do fission yeast (Yaffe et al, 2003), whereas actin is predominantly used by both plants and budding yeast . There is even evidence that mitochondria use intermediate filaments in 3T3 fibroblast cells for proper motility regulation (Nekrasova et al, 2011). Thus, we analyzed D. discoideum mitochondria to establish whether microtubules or actin filaments were utilized for proper motility.…”

“…The cytoskeleton, in addition to affecting mitochondrial morphology plays a crucial role in maintaining mitochondrial distribution throughout the cell by facilitating organelle transport to areas with high metabolic demands Bereiter-Hahn et al, 2008;Kostal and Arriaga, 2011;Nekrasova et al, 2011;Wu et al, 2013). In order to rapidly respond to cellular demands, the cytoskeleton must have a communication system allowing it to influence organelle transport and position.…”

Structural and biomechanical basis of mitochondrial movement in eukaryotic cells

“…For example, it has been proved that vimentin intermediate filaments join the mitochondrial binding with the N-end and inhibit mitochondrial movement. 39 Being an intermediate filament protein, desmin can affect distribution of mitochondria in the striated muscle cell, but inhibits mitochondrial recruitment of kinesin in the cardiac muscle cell. 40 …”