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First published online 11 July 2006
doi: 10.1242/jcs.03026

Journal of Cell Science 119, 3098-3106 (2006)
Published by The Company of Biologists 2006
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Research Article

Fis1p and Caf4p, but not Mdv1p, determine the polar localization of Dnm1p clusters on the mitochondrial surface

Astrid C. Schauss, Jörg Bewersdorf* and Stefan Jakobs{ddagger}

Max-Planck Institute for Biophysical Chemistry, Department of NanoBiophotonics, Am Fassberg 11, 37077 Göttingen, Germany

{ddagger} Author for correspondence (e-mail: sjakobs{at}gwdg.de)

Accepted 27 April 2006

The mitochondrial division machinery consists of the large dynamin-related protein Dnm1p (Drp1/Dlp1 in humans), and Fis1p, Mdv1p and Caf4p. Proper assembly of Dnm1p complexes on the mitochondrial surface is crucial for balanced fission and fusion events. Using quantitative confocal microscopy, we show that Caf4p is important for the recruitment of Dnm1p to the mitochondria. The mitochondrial Dnm1p assemblies can be divided into at least two morphologically distinguishable fractions. A small subset of these assemblies appear to be present as Dnm1p-spirals (or rings) that encircle tubule constrictions, with seldom more than seven turns. A larger fraction of the Dnm1p assemblies is primarily present at one side of the mitochondrial tubules. We show that a majority of these mitochondria-associated Dnm1p clusters point towards the cell cortex. This polarized orientation is abolished in fis1{Delta} and caf4{Delta} yeast cells, but is maintained in mdv1{Delta} cells and after disruption of the actin cytoskeleton. This study suggests that Caf4p plays a key role in determining the polarized localization of those Dnm1p clusters that are not immediately involved in the mitochondrial fission process.

Key words: Actin, Dnm1, Dynamin, Fluorescence microscopy, Mitochondrial fission, Polarity


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