Klp2-mediated Rsp1-Mto1 colocalization inhibits microtubule-dependent microtubule assembly in fission yeast

IF 11.7 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Lingyun Nie, Wenyue Liu, Zhuobi Liang, Fan Zheng, Xing Liu, Xuebiao Yao, Shengqi Xiang, Kai Jiang, Shengnan Zheng, Chuanhai Fu
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引用次数: 0

Abstract

Microtubule assembly takes place at the centrosome and noncentrosomal microtubule–organizing centers (MTOCs). However, the mechanisms controlling the activity of noncentrosomal MTOCs are poorly understood. Here, using the fission yeast Schizosaccharomyces pombe as a model organism, we demonstrate that the kinesin-14 motor Klp2 interacts with the J-domain Hsp70/Ssa1 cochaperone Rsp1, an inhibitory factor of microtubule assembly, and that Klp2 is required for the proper localization of Rsp1 to microtubules. In addition, we demonstrate that Klp2 is not required for the localization of Mto1, a factor promoting microtubule assembly, to microtubules. Moreover, Rsp1-Ssa1 inhibits the interaction of Mto1-Mto2 with the gamma-tubulin small complex. The absence of Klp2 reduces the colocalization of Rsp1 and Mto1 foci on preexisting microtubules, resulting in an increased microtubule-dependent microtubule assembly. Our results suggest that Klp2 regulates the activity of noncentrosomal MTOCs by targeting Rsp1 to the sites of Mto1 activity and reveal a mechanism for the inhibition of noncentrosomal microtubule assembly by a kinesin-14 motor.
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来源期刊
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
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