title: Microtubule-organizing center formation at telomeres induces meiotic telomere clustering.
abstract: During meiosis, telomeres cluster and promote homologous chromosome pairing. Telomere clustering requires the interaction of telomeres with the nuclear membrane proteins SUN (Sad1/UNC-84) and KASH (Klarsicht/ANC-1/Syne homology). The mechanism by which telomeres gather remains elusive. In this paper, we show that telomere clustering in fission yeast depends on microtubules and the microtubule motors, cytoplasmic dynein, and kinesins. Furthermore, the γ-tubulin complex (γ-TuC) is recruited to SUN- and KASH-localized telomeres to form a novel microtubule-organizing center that we termed the "telocentrosome." Telocentrosome formation depends on the γ-TuC regulator Mto1 and on the KASH protein Kms1, and depletion of either Mto1 or Kms1 caused severe telomere clustering defects. In addition, the dynein light chain (DLC) contributes to telocentrosome formation, and simultaneous depletion of DLC and dynein also caused severe clustering defects. Thus, the telocentrosome is essential for telomere clustering. We propose that telomere-localized SUN and KASH induce telocentrosome formation and that subsequent microtubule motor-dependent aggregation of telocentrosomes via the telocentrosome-nucleated microtubules causes telomere clustering.
authors: Department of Chemistry, Shizuoka University, Suruga-ku, Shizuoka 422-8529, Japan.
authors: Masashi
authors: M
authors: Yoshida
authors: Satoshi
authors: S
authors: Katsuyama
authors: Kazuki
authors: K
authors: Tateho
authors: Hiroto
authors: H
authors: Nakamura
authors: Junpei
authors: J
authors: Miyoshi
authors: Tatsunori
authors: T
authors: Ohba
authors: Hirotada
authors: H
authors: Matsuhara
authors: Futaba
authors: F
authors: Miki
authors: Koei
authors: K
authors: Okazaki
authors: Tokuko
authors: T
authors: Haraguchi
authors: Osami
authors: O
authors: Niwa
authors: Yasushi
authors: Y
authors: Hiraoka
authors: Ayumu
authors: A
authors: Yamamoto
mesh_terms: D056445:Cytoplasmic Dyneins / Q000235:genetics / Q000502:physiology*; D017353:Gene Deletion; D008540:Meiosis / Q000235:genetics*; D022101:Microtubule-Organizing Center / Q000378:metabolism* / Q000648:ultrastructure; D008870:Microtubules / Q000378:metabolism / Q000502:physiology / Q000648:ultrastructure; D008954:Models, Biological; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D029702:Schizosaccharomyces pombe Proteins / Q000378:metabolism / Q000502:physiology; D016615:Telomere / Q000378:metabolism* / Q000648:ultrastructure; D034501:Telomere-Binding Proteins / Q000378:metabolism / Q000502:physiology
chemical_list: C510171:Bqt1 protein, S pombe; C510172:Bqt2 protein, S pombe; C093512:SAD1 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; D034501:Telomere-Binding Proteins; D056445:Cytoplasmic Dyneins
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