Pex19p Contributes to Peroxisome Inheritance in the Association of Peroxisomes to Myo2p

Authors

  • Marleen Otzen,

    1. Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Kluyver Centre for Genomics of Industrial Fermentation, University of Groningen, Groningen, the Netherlands
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  • Robert Rucktäschel,

    1. Institute of Physiological Chemistry, Medical Faculty, Ruhr-University-Bochum, Bochum, Germany
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  • Sven Thoms,

    1. Institute of Physiological Chemistry, Medical Faculty, Ruhr-University-Bochum, Bochum, Germany
    2. Current address: Department of Pediatrics and Pediatric Neurology, University Medical Center, University of Göttingen, Göttingen, Germany
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  • Kerstin Emmrich,

    1. Institute of Physiological Chemistry, Medical Faculty, Ruhr-University-Bochum, Bochum, Germany
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  • Arjen M. Krikken,

    1. Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Kluyver Centre for Genomics of Industrial Fermentation, University of Groningen, Groningen, the Netherlands
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  • Ralf Erdmann,

    1. Institute of Physiological Chemistry, Medical Faculty, Ruhr-University-Bochum, Bochum, Germany
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  • Ida J. van der Klei

    Corresponding author
    • Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Kluyver Centre for Genomics of Industrial Fermentation, University of Groningen, Groningen, the Netherlands
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Corresponding author: Ida. J. van der Klei, I.J.van.der.klei@rug.nl

Abstract

During budding of yeast cells peroxisomes are distributed over mother cell and bud, a process that involves the myosin motor protein Myo2p and the peroxisomal membrane protein Inp2p. Here, we show that Pex19p, a peroxin implicated in targeting and complex formation of peroxisomal membrane proteins, also plays a role in peroxisome partitioning. Binding studies revealed that Pex19p interacts with the cargo-binding domain of Myo2p. We identified mutations in Myo2p that specifically reduced binding to Pex19p, but not to Inp2p. The interaction between Myo2p and Pex19p was also reduced by a mutation that blocked Pex19p farnesylation. Microscopy revealed that the Pex19p–Myo2p interaction is important for peroxisome inheritance, because mutations that affect this interaction hamper peroxisome inheritance in vivo. Together these data suggest that both Inp2p and Pex19p are required for proper association of peroxisomes to Myo2p.

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