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Published online
doi:10.1083/jcb.200904050
The Journal of Cell Biology, Vol. 186, No. 4, 541-554
The Rockefeller University Press, 0021-9525 $30.00
© Fagarasanu et al.
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Article

Myosin-driven peroxisome partitioning in S. cerevisiae



Andrei Fagarasanu1, Fred D. Mast1, Barbara Knoblach1, Yui Jin3, Matthew J. Brunner3, Michael R. Logan1, J.N. Mark Glover2, Gary A. Eitzen1, John D. Aitchison4, Lois S. Weisman3, and Richard A. Rachubinski1

1 Department of Cell Biology and 2 Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
3 Life Sciences Institute, Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109
4 Institute for Systems Biology, Seattle, WA 98103

Correspondence to Richard A. Rachubinski: rick.rachubinski{at}ualberta.ca

In Saccharomyces cerevisiae, the class V myosin motor Myo2p propels the movement of most organelles. We recently identified Inp2p as the peroxisome-specific receptor for Myo2p. In this study, we delineate the region of Myo2p devoted to binding peroxisomes. Using mutants of Myo2p specifically impaired in peroxisome binding, we dissect cell cycle–dependent and peroxisome partitioning–dependent mechanisms of Inp2p regulation. We find that although total Inp2p levels oscillate with the cell cycle, Inp2p levels on individual peroxisomes are controlled by peroxisome inheritance, as Inp2p aberrantly accumulates and decorates all peroxisomes in mother cells when peroxisome partitioning is abolished. We also find that Inp2p is a phosphoprotein whose level of phosphorylation is coupled to the cell cycle irrespective of peroxisome positioning in the cell. Our findings demonstrate that both organelle positioning and cell cycle progression control the levels of organelle-specific receptors for molecular motors to ultimately achieve an equidistribution of compartments between mother and daughter cells.

Abbreviations used in this paper: CSM, complete supplement mixture; G6PDH, glucose-6-phosphate dehydrogenase; MBP, maltose-binding protein; mRFP, monomeric RFP; pA, protein A.

© 2009 Fagarasanu et al.
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Peroxisome inheritance at the right time and place
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