KIF14 binds tightly to microtubules and adopts a rigor-like conformation.

  title={KIF14 binds tightly to microtubules and adopts a rigor-like conformation.},
  author={Kritica Arora and Lama Talje and A. Asenjo and P. Andersen and Kaleem Atchia and M. Joshi and H. Sosa and J. Allingham and B. Kwok},
  journal={Journal of molecular biology},
  volume={426 17},
  • Kritica Arora, Lama Talje, +6 authors B. Kwok
  • Published 2014
  • Biology, Medicine
  • Journal of molecular biology
  • The mitotic kinesin motor protein KIF14 is essential for cytokinesis during cell division and has been implicated in cerebral development and a variety of human cancers. Here we show that the mouse KIF14 motor domain binds tightly to microtubules and does not display typical nucleotide-dependent changes in this affinity. It also has robust ATPase activity but very slow motility. A crystal structure of the ADP-bound form of the KIF14 motor domain reveals a dramatically opened ATP-binding pocket… CONTINUE READING
    34 Citations
    Kinesin, 30 years later: Recent insights from structural studies
    • 27
    Kinesin expands and stabilises the GDP-microtubule lattice
    • 32
    • PDF
    Intrinsically disordered domain of kinesin-3 Kif14 enables unique functional diversity
    • 1
    • PDF
    Kinesin motility is driven by subdomain dynamics
    • 11
    • PDF
    High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation
    • 96
    • Highly Influenced
    • PDF
    Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
    • 18
    • PDF


    Large conformational changes in a kinesin motor catalyzed by interaction with microtubules.
    • 82
    • PDF
    A seesaw model for intermolecular gating in the kinesin motor protein
    • 40
    • PDF
    Switch-based mechanism of kinesin motors
    • 303
    • Highly Influential
    KIF1A Alternately Uses Two Loops to Bind Microtubules
    • 156
    • Highly Influential
    Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • 170
    Monomeric and dimeric states exhibited by the kinesin-related motor protein KIF1A.
    • 31
    Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules
    • 88
    • PDF
    An atomic-level mechanism for activation of the kinesin molecular motors
    • 145
    • PDF
    Allosteric control of kinesin's motor domain by tubulin: a molecular dynamics study.
    • 10
    • PDF
    High‐resolution cryo‐EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
    • 104
    • Highly Influential
    • PDF