Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute-GBB, Kluyver Centre for Genomics of Industrial Fermentation, University of Groningen, Groningen, the Netherlands.
Traffic. 2012 Jul;13(7):947-59. doi: 10.1111/j.1600-0854.2012.01364.x. Epub 2012 Apr 26.
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.
在酵母细胞出芽过程中,过氧化物酶体分布在母细胞和芽上,这一过程涉及肌球蛋白马达蛋白 Myo2p 和过氧化物酶体膜蛋白 Inp2p。在这里,我们表明,参与过氧化物酶体膜蛋白靶向和复合物形成的过氧化物酶体蛋白 Pex19p 也在过氧化物酶体分配中发挥作用。结合研究表明 Pex19p 与 Myo2p 的货物结合结构域相互作用。我们鉴定了 Myo2p 中的突变,这些突变特异性降低了与 Pex19p 的结合,但不降低与 Inp2p 的结合。阻断 Pex19p 法呢基化的突变也降低了 Myo2p 和 Pex19p 之间的相互作用。显微镜观察表明,Myo2p 和 Pex19p 之间的相互作用对于过氧化物酶体的遗传是重要的,因为影响这种相互作用的突变会阻碍体内过氧化物酶体的遗传。这些数据表明,Inp2p 和 Pex19p 都需要将过氧化物酶体正确地与 Myo2p 结合。