title: Myosin-driven peroxisome partitioning in S. cerevisiae.
abstract: 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.
authors.affiliation: Department of Cell Biology and 2 Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G2H7, Canada.
authors.forename: Andrei
authors.initials: A
authors.lastname: Fagarasanu
authors.forename: Fred D
authors.initials: FD
authors.lastname: Mast
authors.forename: Barbara
authors.initials: B
authors.lastname: Knoblach
authors.forename: Yui
authors.initials: Y
authors.lastname: Jin
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Brunner
authors.forename: Michael R
authors.initials: MR
authors.lastname: Logan
authors.forename: J N Mark
authors.initials: JN
authors.lastname: Glover
authors.forename: Gary A
authors.initials: GA
authors.lastname: Eitzen
authors.forename: John D
authors.initials: JD
authors.lastname: Aitchison
authors.forename: Lois S
authors.initials: LS
authors.lastname: Weisman
authors.forename: Richard A
authors.initials: RA
authors.lastname: Rachubinski
mesh_terms: D002453:Cell Cycle / Q000502:physiology*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D018995:Myosin Heavy Chains / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D024701:Myosin Type V / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020675:Peroxisomes / Q000378:metabolism*; D017354:Point Mutation; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020798:Two-Hybrid System Techniques; D014617:Vacuoles / Q000378:metabolism
chemical_list: C510742:INP2 protein, S cerevisiae; C077512:MYO2 protein, S cerevisiae; D008565:Membrane Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D024701:Myosin Type V; D018995:Myosin Heavy Chains
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