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¹ Lehrstuhl für Angewandte Mikrobiologie, Biozentrum, Universität Basel, CH-4056 Basel, Switzerland
² Department of Biochemistry, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, Netherlands

Address correspondence to Department of Biochemistry, Academic Medical Center, University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, Netherlands. Tel.: (31) 20-566-5127. Fax: (31) 20-691-5519. E-mail: h.f.tabak{at}amc.uva.nl

In vivo time-lapse microscopy reveals that the number of peroxisomes in Saccharomyces cerevisiae cells is fairly constant and that a subset of the organelles are targeted and segregated to the bud in a highly ordered, vectorial process. The dynamin-like protein Vps1p controls the number of peroxisomes, since in a vps1 mutant only one or two giant peroxisomes remain. Analogous to the function of other dynamin-related proteins, Vps1p may be involved in a membrane fission event that is required for the regulation of peroxisome abundance. We found that efficient segregation of peroxisomes from mother to bud is dependent on the actin cytoskeleton, and active movement of peroxisomes along actin filaments is driven by the class V myosin motor protein, Myo2p: (a) peroxisomal dynamics always paralleled the polarity of the actin cytoskeleton, (b) double labeling of peroxisomes and actin cables revealed a close association between both, (c) depolymerization of the actin cytoskeleton abolished all peroxisomal movements, and (d) in cells containing thermosensitive alleles of MYO2, all peroxisome movement immediately stopped at the nonpermissive temperature. In addition, time-lapse videos showing peroxisome movement in wild-type and vps1 cells suggest the existence of various levels of control involved in the partitioning of peroxisomes.

Key Words: peroxisome inheritance; Vps1; fission; actin cytoskeleton; Myo2p

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