CLASP-mediated competitive binding in protein condensates directs microtubule growth

Xuanyan Jia, Leishu Lin, Siqi Guo, Lulu Zhou, Gaowei Jin, Jiayuan Dong, Jinman Xiao, Xingqiao Xie, Yiming Li, Sicong He, Zhiyi Wei () and Cong Yu ()
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Xuanyan Jia: Shenzhen Key Laboratory of Biomolecular Assembling and Regulation
Leishu Lin: Shenzhen Key Laboratory of Biomolecular Assembling and Regulation
Siqi Guo: Southern University of Science and Technology
Lulu Zhou: Southern University of Science and Technology
Gaowei Jin: Southern University of Science and Technology
Jiayuan Dong: Shenzhen Key Laboratory of Biomolecular Assembling and Regulation
Jinman Xiao: Southern University of Science and Technology
Xingqiao Xie: Shenzhen Key Laboratory of Biomolecular Assembling and Regulation
Yiming Li: Southern University of Science and Technology
Sicong He: Southern University of Science and Technology
Zhiyi Wei: Shenzhen Key Laboratory of Biomolecular Assembling and Regulation
Cong Yu: Southern University of Science and Technology

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Microtubule organization in cells relies on targeting mechanisms. Cytoplasmic linker proteins (CLIPs) and CLIP-associated proteins (CLASPs) are key regulators of microtubule organization, yet the underlying mechanisms remain elusive. Here, we reveal that the C-terminal domain of CLASP2 interacts with a common motif found in several CLASP-binding proteins. This interaction drives the dynamic localization of CLASP2 to distinct cellular compartments, where CLASP2 accumulates in protein condensates at the cell cortex or the microtubule plus end. These condensates physically contact each other via CLASP2-mediated competitive binding, determining cortical microtubule targeting. The phosphorylation of CLASP2 modulates the dynamics of the condensate-condensate interaction and spatiotemporally navigates microtubule growth. Moreover, we identify additional CLASP-interacting proteins that are involved in condensate contacts in a CLASP2-dependent manner, uncovering a general mechanism governing microtubule targeting. Our findings not only unveil a tunable multiphase system regulating microtubule organization, but also offer general mechanistic insights into intricate protein-protein interactions at the mesoscale level.

Date: 2024
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DOI: 10.1038/s41467-024-50863-3

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