title: An ER-peroxisome tether exerts peroxisome population control in yeast.
abstract: Eukaryotic cells compartmentalize biochemical reactions into membrane-enclosed organelles that must be faithfully propagated from one cell generation to the next. Transport and retention processes balance the partitioning of organelles between mother and daughter cells. Here we report the identification of an ER-peroxisome tether that links peroxisomes to the ER and ensures peroxisome population control in the yeast Saccharomyces cerevisiae. The tether consists of the peroxisome biogenic protein, Pex3p, and the peroxisome inheritance factor, Inp1p. Inp1p bridges the two compartments by acting as a molecular hinge between ER-bound Pex3p and peroxisomal Pex3p. Asymmetric peroxisome division leads to the formation of Inp1p-containing anchored peroxisomes and Inp1p-deficient mobile peroxisomes that segregate to the bud. While peroxisomes in mother cells are not released from tethering, de novo formation of tethers in the bud assists in the directionality of peroxisome transfer. Peroxisomes are thus stably maintained over generations of cells through their continued interaction with tethers.
authors.affiliation: Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada.
authors.forename: Barbara
authors.initials: B
authors.lastname: Knoblach
authors.forename: Xuejun
authors.initials: X
authors.lastname: Sun
authors.forename: Nicolas
authors.initials: N
authors.lastname: Coquelle
authors.forename: Andrei
authors.initials: A
authors.lastname: Fagarasanu
authors.forename: Richard L
authors.initials: RL
authors.lastname: Poirier
authors.forename: Richard A
authors.initials: RA
authors.lastname: Rachubinski
mesh_terms: D002455:Cell Division / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics; D000074401:Peroxins; D020675:Peroxisomes / Q000378:metabolism*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: C502615:INP1 protein, S cerevisiae; D008565:Membrane Proteins; C070895:PEX3 protein, S cerevisiae; D000074401:Peroxins; D029701:Saccharomyces cerevisiae Proteins
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