Myosin-driven peroxisome partitioning in S. cerevisiae
Autor: | Fred D. Mast, Gary Eitzen, Michael Logan, J. N. Mark Glover, Barbara Knoblach, Richard A. Rachubinski, Andrei Fagarasanu, John D. Aitchison, Lois S. Weisman, Yui Jin, Matthew J. Brunner |
---|---|
Rok vydání: | 2009 |
Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Cell division Recombinant Fusion Proteins Myosin Type V Saccharomyces cerevisiae Peroxisome inheritance Receptors Cytoplasmic and Nuclear Vacuole Article 03 medical and health sciences 0302 clinical medicine Two-Hybrid System Techniques Organelle Myosin Peroxisomes Point Mutation Research Articles 030304 developmental biology 0303 health sciences Molecular Structure Myosin Heavy Chains biology Cell Cycle Membrane Proteins Cell Biology Cell cycle Peroxisome biology.organism_classification Mitochondria Protein Structure Tertiary Cell biology Biochemistry Vacuoles Protein Processing Post-Translational 030217 neurology & neurosurgery |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
DOI: | 10.1083/jcb.200904050 |
Popis: | 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. |
Databáze: | OpenAIRE |
Externí odkaz: |