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Pushing for answers: is myosin V directly involved in moving mitochondria?

ABSTRACT: In budding yeast, the actin-based class V myosin motors, Myo2 and Myo4, transport virtually all organelles from mother to bud during cell division. Until recently, it appeared that mitochondria may be an exception, with studies showing that the Arp2/3 complex is required for their movement. However, several recent studies have proposed that Myo2 has a direct involvement in mitochondria inheritance. In this issue, Altmann et al. (Altmann, K., M. Frank, D. Neumann, S. Jakobs, and B. Westermann. 2008. J. Cell Biol. 181:119-130) provide the strongest support yet that Myo2 and its associated light chain Mlc1 function directly and significantly in both mitochondria-actin interactions and in the movement of mitochondria from mother to bud. The conflicting functions of Arp 2/3 and Myo2 may be reconciled by the existence of multiple pathways involved in mitochondrial transport.

SUBMITTER: Valiathan RR

PROVIDER: S-EPMC2287276 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

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Pushing for answers: is myosin V directly involved in moving mitochondria?

Valiathan Rajeshwari R RR Weisman Lois S LS

The Journal of cell biology 20080401 1

In budding yeast, the actin-based class V myosin motors, Myo2 and Myo4, transport virtually all organelles from mother to bud during cell division. Until recently, it appeared that mitochondria may be an exception, with studies showing that the Arp2/3 complex is required for their movement. However, several recent studies have proposed that Myo2 has a direct involvement in mitochondria inheritance. In this issue, Altmann et al. (Altmann, K., M. Frank, D. Neumann, S. Jakobs, and B. Westermann. 20 ...[more]

PMID: 18391069

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Project description:Although the mechanisms by which mutant huntingtin (mHtt) results in Huntington's disease (HD) remain unclear, mHtt-induced mitochondrial defects were implicated in HD pathogenesis. The effect of mHtt could be mediated by transcriptional alterations, by direct interaction with mitochondria, or by both. In the present study, we tested a hypothesis that mHtt directly damages mitochondria. To test this hypothesis, we applied brain cytosolic fraction from YAC128 mice, containing mHtt, to brain non-synaptic and synaptic mitochondria from wild-type mice and assessed mitochondrial respiration with a Clark-type oxygen electrode, membrane potential and Ca2+ uptake capacity with tetraphenylphosphonium (TPP+ )- and Ca2+ -sensitive electrodes, respectively, and, reactive oxygen species production with Amplex Red assay. The amount of mHtt bound to mitochondria following incubation with mHtt-containing cytosolic fraction was greater than the amount of mHtt bound to brain mitochondria isolated from YAC128 mice. Despite mHtt binding to wild-type mitochondria, no abnormalities in mitochondrial functions were detected. This is consistent with our previous results demonstrating the lack of defects in brain mitochondria isolated from R6/2 and YAC128 mice. This, however, could be because of partial loss of mitochondrially bound mHtt during the isolation procedure. Consequently, we increased the amount of mitochondrially bound mHtt by incubating brain non-synaptic and synaptic mitochondria isolated from YAC128 mice with mHtt-containing cytosolic fraction. Despite the enrichment of YAC128 brain mitochondria with mHtt, mitochondrial functions (respiration, membrane potential, reactive oxygen species production, Ca2+ uptake capacity) remained unchanged. Overall, our results suggest that mHtt does not directly impair mitochondrial functions, arguing against the involvement of this mechanism in HD pathogenesis. Open Science: This manuscript was awarded with the Open Materials Badge For more information see: https://cos.io/our-services/open-science-badges/.

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Pushing for answers: is myosin V directly involved in moving mitochondria?

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Pushing for answers: is myosin V directly involved in moving mitochondria?

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