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Published online July 7, 2008
doi:10.1083/jcb.200712147
The Journal of Cell Biology, Vol. 182, No. 1, 41-49
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Chiron et al.
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 CLASP regulates mitochondrial distribution in Schizosaccharomyces pombe

Stéphane Chiron, Alyona Bobkova, Haowen Zhou, and Michael P. Yaffe

Section of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093

Correspondence to Stéphane Chiron: schiron{at}gmail.com

Movement of mitochondria in Schizosaccharomyces pombe depends on their association with the dynamic, or plus ends, of microtubules, yet the molecular basis for this interaction is poorly understood. We identified mmd4 in a screen of temperature-sensitive S. pombe strains for aberrant mitochondrial morphology and distribution. Cells with the mmd4 mutation display mitochondrial aggregation near the cell ends at elevated temperatures, a phenotype similar to mitochondrial defects observed in wild-type cells after microtubule depolymerization. However, microtubule morphology and function appear normal in the mmd4 mutant. The mmd4 lesion maps to peg1+, which encodes a microtubule-associated protein with homology to cytoplasmic linker protein–associated proteins (mammalian microtubule plus end–binding proteins). Peg1p localizes to the plus end of microtubules and to mitochondria and is recovered with mitochondria during subcellular fractionation. This mitochondrial-associated fraction of Peg1p displays properties of a peripherally associated protein. Peg1p is the first identified microtubule plus end–binding protein required for mitochondrial distribution and likely functions as a molecular link between mitochondria and microtubules.

Abbreviations used in this paper: +TIP, plus end–tracking protein; HSP, high speed pellet; SPB, spindle pole body; ts, temperature sensitive.


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