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Krenn V.,Max Planck Institute of Molecular Physiology | Krenn V.,IMBA Institute for Molecular Biotechnology | Musacchio A.,Max Planck Institute of Molecular Physiology | Musacchio A.,University of Duisburg - Essen
Frontiers in Oncology | Year: 2015

Aurora B, a member of the Aurora family of serine/threonine protein kinases, is a key player in chromosome segregation. As part of a macromolecular complex known as the chromosome passenger complex, Aurora B concentrates early during mitosis in the proximity of centromeres and kinetochores, the sites of attachment of chromosomes to spindle microtubules. There, it contributes to a number of processes that impart fidelity to cell division, including kinetochore stabilization, kinetochore-microtubule attachment, and the regulation of a surveillance mechanism named the spindle assembly checkpoint. In the regulation of these processes, Aurora B is the fulcrum of a remarkably complex network of interactions that feed back on its localization and activation state. In this review, we discuss the multiple roles of Aurora B during mitosis, focusing in particular on its role at centromeres and kinetochores. Many details of the network of interactions at these locations remain poorly understood, and we focus here on several crucial outstanding questions. © 2015 Krenn and Musacchio. Source


Leitner A.,University of Vienna | Sturm M.,University of Vienna | Hudecz O.,IMP Research Institute of Molecular Pathology | Hudecz O.,IMBA Institute for Molecular Biotechnology | And 7 more authors.
Analytical Chemistry | Year: 2010

Metal oxide affinity chromatography (MOAC) has become a prominent method to enrich phosphopeptides prior to their analysis by liquid chromatography-mass spectrometry. To overcome limitations in material design, we have previously reported the use of nanocasting as a means to generate metal oxide spheres with tailored properties. Here, we report on the application of two oxides, tin dioxide (stannia) and titanium dioxide (titania), for the analysis of the HeLa phosphoproteome. In combination with nanoflow LC-MS/MS analysis on a linear ion trapFourier transform ion cyclotron resonance instrument, we identified 619 phosphopeptides using the new stannia material, and 896 phosphopeptides using titania prepared in house. We also compared the newly developed materials to commercial titania material using an established enrichment protocol. Both titania materials yielded a comparable total number of phosphopeptides, but the overlap of the two data sets was less than one-third. Although fewer peptides were identified using stannia, the complementarity of SnO2-based MOAC could be shown as more than 140 phosphopeptides were exclusively identified by this material. © 2010 American Chemical Society. Source

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