HURP facilitates spindle assembly by stabilizing microtubules and working synergistically with TPX2

Venecia Alexandria Valdez, Meisheng Ma, Bernardo Gouveia, Rui Zhang () and Sabine Petry ()
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Venecia Alexandria Valdez: Princeton University
Meisheng Ma: School of Medicine
Bernardo Gouveia: Princeton University
Rui Zhang: School of Medicine
Sabine Petry: Princeton University

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract In vertebrate spindles, most microtubules are formed via branching microtubule nucleation, whereby microtubules nucleate along the side of pre-existing microtubules. Hepatoma up-regulated protein (HURP) is a microtubule-associated protein that has been implicated in spindle assembly, but its mode of action is yet to be defined. In this study, we show that HURP is necessary for RanGTP-induced branching microtubule nucleation in Xenopus egg extract. Specifically, HURP stabilizes the microtubule lattice to promote microtubule formation from γ-TuRC. This function is shifted to promote branching microtubule nucleation through enhanced localization to TPX2 condensates, which form the core of the branch site on microtubules. Lastly, we provide a high-resolution cryo-EM structure of HURP on the microtubule, revealing how HURP binding stabilizes the microtubule lattice. We propose a model in which HURP stabilizes microtubules during their formation, and TPX2 preferentially enriches HURP to microtubules to promote branching microtubule nucleation and thus spindle assembly.

Date: 2024
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DOI: 10.1038/s41467-024-53630-6

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