title: Fission yeast mitochondria are distributed by dynamic microtubules in a motor-independent manner.
abstract: The cytoskeleton plays a critical role in regulating mitochondria distribution. Similar to axonal mitochondria, the fission yeast mitochondria are distributed by the microtubule cytoskeleton, but this is regulated by a motor-independent mechanism depending on the microtubule associated protein mmb1p as the absence of mmb1p causes mitochondria aggregation. In this study, using a series of chimeric proteins to control the subcellular localization and motility of mitochondria, we show that a chimeric molecule containing a microtubule binding domain and the mitochondria outer membrane protein tom22p can restore the normal interconnected mitochondria network in mmb1-deletion (mmb1∆) cells. In contrast, increasing the motility of mitochondria by using a chimeric molecule containing a kinesin motor domain and tom22p cannot rescue mitochondria aggregation defects in mmb1∆ cells. Intriguingly a chimeric molecule carrying an actin binding domain and tom22p results in mitochondria associated with actin filaments at the actomyosin ring during mitosis, leading to cytokinesis defects. These findings suggest that the passive motor-independent microtubule-based mechanism is the major contributor to mitochondria distribution in wild type fission yeast cells. Hence, we establish that attachment to microtubules, but not kinesin-dependent movement and the actin cytoskeleton, is required and crucial for proper mitochondria distribution in fission yeast.
authors.affiliation: 1] Department of Biochemistry [2] HKU-Shenzhen Institute of Research and Innovation, The University of Hong Kong, Shenzhen, China.
authors.forename: Tianpeng
authors.initials: T
authors.lastname: Li
authors.affiliation: 1] Department of Biochemistry [2] HKU-Shenzhen Institute of Research and Innovation, The University of Hong Kong, Shenzhen, China.
authors.forename: Fan
authors.initials: F
authors.lastname: Zheng
authors.affiliation: Department of Anatomy, The University of Hong Kong, Pokfulam, Hong Kong, China.
authors.forename: Martin
authors.initials: M
authors.lastname: Cheung
authors.affiliation: School of Life Sciences, Anhui Medical University, Hefei, Anhui 230032, China.
authors.forename: Fengsong
authors.initials: F
authors.lastname: Wang
authors.affiliation: 1] Department of Biochemistry [2] HKU-Shenzhen Institute of Research and Innovation, The University of Hong Kong, Shenzhen, China.
authors.forename: Chuanhai
authors.initials: C
authors.lastname: Fu
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D048749:Cytokinesis / Q000502:physiology; D008856:Microscopy, Fluorescence; D008870:Microtubules / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D008938:Mitosis; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D012568:Schizosaccharomyces / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D011993:Recombinant Fusion Proteins; D029702:Schizosaccharomyces pombe Proteins