Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p
Links to Fileshttps://www.cell.com/cell/fulltext/S0092-8674(02)00973-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS009286740200973X%3Fshowall%3Dtrue
MetadataShow full item record
Type of Work10 pages
Citation of Original PublicationCheeseman, Iain M et al. “Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p.” Cell vol. 111,2 (2002): 163-72. doi:10.1016/s0092-8674(02)00973-x
RightsThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
The Aurora kinase Ipl1p plays a crucial role in regulating kinetochore-microtubule attachments in budding yeast, but the underlying basis for this regulation is not known. To identify Ipl1p targets, we first purified 28 kinetochore proteins from yeast protein extracts. These studies identified five previously uncharacterized kinetochore proteins and defined two additional kinetochore subcomplexes. We then used mass spectrometry to identify 18 phosphorylation sites in 7 of these 28 proteins. Ten of these phosphorylation sites are targeted directly by Ipl1p, allowing us to identify a consensus phosphorylation site for an Aurora kinase. Our systematic mutational analysis of the Ipl1p phosphorylation sites demonstrated that the essential microtubule binding protein Dam1p is a key Ipl1p target for regulating kinetochore-microtubule attachments in vivo.