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First published online July 25, 2006

Journal of Cell Science 119, 1505e (2006)
© The Company of Biologists Limited
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In this issue

Caf4p nets mitochondria


Figure 1

In many organisms, mitochondria form dynamic networks that continually undergo fission and fusion. In budding yeast, the large dynamin-related GTPase Dnm1p is central to mitochondrial fission. The integral mitochondrial membrane protein Fis1p targets Dnm1p to the mitochondrial surface through the WD40 proteins Caf4p and Mdv1p. These protein assemblies are thought to form spiral structures around constricted mitochondrial tubules that drive mitochondrial division. On p. 3098, Stefan Jakobs and co-authors use quantitative fluorescence microscopy to study two morphologically distinguishable (but probably interconvertible) types of Dnm1p assembly in yeast mitochondria: spirals that encircle tubule constrictions; and clusters that are present at only one side of the tubules. The latter, more common structure is mostly orientated towards the cell cortex and its polarity depends on Fis1p and Caf4p but not Mdv1p. The authors suggest that the polarity of the non-spiral Dnm1p clusters is due to their physical attachment to the cell cortex through Caf4p. By creating such attachments, Caf1p might help to establish the normal dynamic mitochondrial network.


Related articles in JCS:

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
JCS 2006 119: 3098-3106. [Abstract] [Full Text]  




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