Yeast GSK-3 kinase regulates astral microtubule function via phosphorylation of the microtubule-stabilizing kinesin Kip2

Author:

Drechsler Hauke1,Tan Ann Na1,Liakopoulos Dimitris1

Affiliation:

1. Biochemistry Centre Heidelberg (BZH), INF 328, 69120 Heidelberg, Germany

Abstract

The S. cerevisiae kinesin Kip2 stabilises astral microtubules and facilitates spindle positioning through transport of microtubule-associated proteins, such as the yeast CLIP-170 homologue Bik1, dynein and the Adenomatous Polyposis Coli-related protein Kar9 to the plus ends of astral microtubules. Here, we show that Kip2 associates physically with its processivity factor Bim1, the yeast homologue of the EB1 plus end-tracking protein. This interaction requires an EB1-binding motif in the N-terminal extension of Kip2 and is negatively regulated by phosphorylation through Mck1, the yeast Glycogen Synthase Kinase 3. In addition, Mck1-dependent phosphorylation decreases the intrinsic microtubule affinity of Kip2. Reduction in Kip2 phosphorylation leads to stabilisation of astral microtubules and accumulation of Kip2, dynein and Kar9 at microtubule plus ends, while loss of Mck1 function leads to defects in spindle positioning. Furthermore, we provide evidence that a subpopulation of Mck1 at the bud-cortex phosphorylates Kip2. We propose that yeast GSK-3 spatially controls astral microtubule dynamics and the loading of dynein and Kar9 on astral microtubule plus ends by regulating Kip2 interactions with Bim1 and microtubules.

Publisher

The Company of Biologists

Subject

Cell Biology

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3