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

Kritica Arora, Lama Talje, Ana B. Asenjo, Parker Andersen, Kaleem Atchia, Monika Joshi, Hernando Sosa, John S. Allingham, Benjamin H. Kwok

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


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, as if ready to exchange its bound ADP for Mg·ATP. In this state, the central β-sheet is twisted ~ 10° beyond the maximal amount observed in other kinesins. This configuration has only been seen in the nucleotide-free states of myosins - known as the "rigor-like" state. Fitting of this atomic model to electron density maps from cryo-electron microscopy indicates a distinct binding configuration of the motor domain to microtubules. We postulate that these properties of KIF14 are well suited for stabilizing midbody microtubules during cytokinesis.

Original languageEnglish (US)
Pages (from-to)2997-3015
Number of pages19
JournalJournal of Molecular Biology
Issue number17
StatePublished - Aug 26 2014


  • KIF14
  • crystal structure
  • kinesin
  • microtubules
  • motor protein

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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