Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation |
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| Authors: | Fan Zheng Tianpeng Li Dong-yan Jin Viktoriya Syrovatkina Kathleen Scheffler Phong T Tran Chuanhai Fu |
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| Institution: | University of North Carolina;aDepartment of Biochemistry, University of Hong Kong, Pokfulam, Hong Kong, China;bHKU-Shenzhen Institute of Research and Innovation, University of Hong Kong, Shenzhen, China;cCell and Developmental Biology, University of Pennsylvania, Philadelphia, PA 10104;dInstitut Curie, Centre National de la Recherche Scientifique, Paris 75005, France |
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| Abstract: | Accurate chromosome segregation requires timely bipolar spindle formation during mitosis. The transforming acidic coiled-coil (TACC) family proteins and the ch-TOG family proteins are key players in bipolar spindle formation. They form a complex to stabilize spindle microtubules, mainly dependent on their localization to the centrosome (the spindle pole body SPB] in yeast). The molecular mechanism underlying the targeting of the TACC–ch-TOG complex to the centrosome remains unclear. Here we show that the fission yeast Schizosaccharomyces pombe TACC orthologue alp7p is recruited to the SPB by csi1p. The csi1p-interacting region lies within the conserved TACC domain of alp7p, and the carboxyl-terminal domain of csi1p is responsible for interacting with alp7p. Compromised interaction between csi1p and alp7p impairs the localization of alp7p to the SPB during mitosis, thus delaying bipolar spindle formation and leading to anaphase B lagging chromosomes. Hence our study establishes that csi1p serves as a linking molecule tethering spindle-stabilizing factors to the SPB for promoting bipolar spindle assembly. |
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