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From Proteopedia
Crystal structure of the mouse Kif14 motor domain
Structural highlights
FunctionKIF14_MOUSE Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (PubMed:24949858). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (By similarity). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (By similarity). Regulates cell growth through regulation of cell cycle progression and cytokinesis. During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (By similarity). During late neurogenesis, regulates the cerebellar and cerebral cortex development and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (PubMed:23308235, PubMed:24931760). Also is required for chromosome congression and alignment during mitotic cell cycle process (By similarity). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (By similarity).[UniProtKB:Q15058][1] [2] [3] Publication Abstract from PubMedThe 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. KIF14 binds tightly to microtubules and adopts a rigor-like conformation.,Arora K, Talje L, Asenjo AB, Andersen P, Atchia K, Joshi M, Sosa H, Allingham JS, Kwok BH J Mol Biol. 2014 Jun 17. pii: S0022-2836(14)00282-4. doi:, 10.1016/j.jmb.2014.05.030. PMID:24949858[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
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Categories: Escherichia coli UMEA 3304-1 | Large Structures | Mus musculus | Allingham JS | Andersen P | Arora K | Asenjo AB | Atchia K | Joshi M | Kwok BH | Sosa H | Talje L
