| First Author | Arora K | Year | 2014 |
| Journal | J Mol Biol | Volume | 426 |
| Issue | 17 | Pages | 2997-3015 |
| PubMed ID | 24949858 | Mgi Jnum | J:215928 |
| Mgi Id | MGI:5607363 | Doi | 10.1016/j.jmb.2014.05.030 |
| Citation | Arora K, et al. (2014) KIF14 binds tightly to microtubules and adopts a rigor-like conformation. J Mol Biol 426(17):2997-3015 |
| abstractText | 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 beta-sheet is twisted ~10 degrees 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. |
