Interaction of CK1δ with γTuSC ensures proper microtubule assembly and spindle positioning.

Autor:	Peng Y; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720., Moritz M; Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158., Han X; Department of Chemical Physiology, Scripps Research Institute, La Jolla, CA 92037., Giddings TH; Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Boulder, CO 80309., Lyon A; Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158., Kollman J; Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158., Winey M; Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Boulder, CO 80309., Yates J 3rd; Department of Chemical Physiology, Scripps Research Institute, La Jolla, CA 92037., Agard DA; Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158., Drubin DG; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720 gbarnes@berkeley.edu drubin@berkeley.edu., Barnes G; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720 gbarnes@berkeley.edu drubin@berkeley.edu.
Jazyk:	angličtina
Zdroj:	Molecular biology of the cell [Mol Biol Cell] 2015 Jul 01; Vol. 26 (13), pp. 2505-18. Date of Electronic Publication: 2015 May 13.
DOI:	10.1091/mbc.E14-12-1627
Abstrakt:	Casein kinase 1δ (CK1δ) family members associate with microtubule-organizing centers (MTOCs) from yeast to humans, but their mitotic roles and targets have yet to be identified. We show here that budding yeast CK1δ, Hrr25, is a γ-tubulin small complex (γTuSC) binding factor. Moreover, Hrr25's association with γTuSC depends on its kinase activity and its noncatalytic central domain. Loss of Hrr25 kinase activity resulted in assembly of unusually long cytoplasmic microtubules and defects in spindle positioning, consistent with roles in regulation of γTuSC-mediated microtubule nucleation and the Kar9 spindle-positioning pathway, respectively. Hrr25 directly phosphorylated γTuSC proteins in vivo and in vitro, and this phosphorylation promoted γTuSC integrity and activity. Because CK1δ and γTuSC are highly conserved and present at MTOCs in diverse eukaryotes, similar regulatory mechanisms are expected to apply generally in eukaryotes. (© 2015 Peng et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).)
Databáze:	MEDLINE
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