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Published online
doi:10.1083/jcb.200709099
The Journal of Cell Biology, Vol. 181, No. 1, 119-130
The Rockefeller University Press, 0021-9525 $30.00
© Altmann et al.
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Article

The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in Saccharomyces cerevisiae



Katrin Altmann1, Martina Frank1, Daniel Neumann3, Stefan Jakobs3, and Benedikt Westermann1,2

1 Institut für Zellbiologie and 2 Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95440 Bayreuth, Germany
3 Abteilung NanoBiophotonik, Max-Planck-Institut für Biophysikalische Chemie, 37077 Göttingen, Germany

Correspondence to B. Westermann: benedikt.westermann{at}uni-bayreuth.de

The actin cytoskeleton is essential for polarized, bud-directed movement of cellular membranes in Saccharomyces cerevisiae and thus ensures accurate inheritance of organelles during cell division. Also, mitochondrial distribution and inheritance depend on the actin cytoskeleton, though the precise molecular mechanisms are unknown. Here, we establish the class V myosin motor protein, Myo2, as an important mediator of mitochondrial motility in budding yeast. We found that mutants with abnormal expression levels of Myo2 or its associated light chain, Mlc1, exhibit aberrant mitochondrial morphology and loss of mitochondrial DNA. Specific mutations in the globular tail of Myo2 lead to aggregation of mitochondria in the mother cell. Isolated mitochondria lacking functional Myo2 are severely impaired in their capacity to bind to actin filaments in vitro. Time-resolved fluorescence microscopy revealed a block of bud-directed anterograde mitochondrial movement in cargo binding–defective myo2 mutant cells. We conclude that Myo2 plays an important and direct role for mitochondrial motility and inheritance in budding yeast.

Abbreviations used in this paper: DIC, differential interference contrast; Dox, doxycycline; mtDNA, mitochondrial DNA; mtGFP, mitochondria-targeted GFP.


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