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9DXC

Model of tubulin dimers used for determining the dimer rise in a taxol-stabilized microtubule-HURP complex

Summary for 9DXC
Entry DOI10.2210/pdb9dxc/pdb
Related9DHZ 9DI0
EMDB information46893
DescriptorTubulin alpha-1B chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
Functional Keywordshurp, tubulin, k-fiber, mitosis, spindle, protein binding
Biological sourceSus scrofa (pig)
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Total number of polymer chains4
Total formula weight202205.80
Authors
Perez-Bertoldi, J.M.,Nogales, E. (deposition date: 2024-10-11, release date: 2025-07-16)
Primary citationPerez-Bertoldi, J.M.,Zhao, Y.,Thawani, A.,Yildiz, A.,Nogales, E.
HURP regulates Kif18A recruitment and activity to synergistically control microtubule dynamics.
Nat Commun, 15:9687-9687, 2024
Cited by
PubMed Abstract: During mitosis, microtubule dynamics are regulated to ensure proper alignment and segregation of chromosomes. The dynamics of kinetochore-attached microtubules are regulated by hepatoma-upregulated protein (HURP) and the mitotic kinesin-8 Kif18A, but the underlying mechanism remains elusive. Using single-molecule imaging in vitro, we demonstrate that Kif18A motility is regulated by HURP. While sparse decoration of HURP activates the motor, higher concentrations hinder processive motility. To shed light on this behavior, we determine the binding mode of HURP to microtubules using cryo-EM. The structure helps rationalize why HURP functions as a microtubule stabilizer. Additionally, HURP partially overlaps with the microtubule-binding site of the Kif18A motor domain, indicating that excess HURP inhibits Kif18A motility by steric exclusion. We also observe that HURP and Kif18A function together to suppress dynamics of the microtubule plus-end, providing a mechanistic basis for how they collectively serve in microtubule length control.
PubMed: 39516196
DOI: 10.1038/s41467-024-53691-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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