Aurora-C kinase supports mitotic progression in the absence of Aurora-B

Genetic disruption of aurora B uncovers an essential role for aurora C during early mammalian development

“…Aurora C is sufficient to drive mitotic progression during early embryonic development As lack of the other CPC components, incenp, survivin or borealin, results in early lethality by E2.5 (Cutts et al, 1999;Uren et al, 2000;Yamanaka et al, 2008), we wondered whether aurora B could be dispensable owing to the presence of other aurora kinases during early embryonic development. Indeed, aurora C has been shown previously to bind other CPC components when overexpressed in specific cell lines (Sasai et al, 2004;Slattery et al, 2009;Slattery et al, 2008;Yan et al, 2005). As depicted in Fig.…”

“…These events seem to be necessary for chromosome condensation although the correlation between H3S10 phosphorylation and the condensation of chromosomes is not fully established (Johansen and Johansen, 2006;Nowak and Corces, 2004;Prigent and Dimitrov, 2003). Less is known about aurora C, which can also bind members of the CPC (Li et al, 2004) and its ectopic expression can rescue aurora B loss of function in cultured cells (Sasai et al, 2004;Slattery et al, 2009;Slattery et al, 2008;Yan et al, 2005). Although aurora C is known to have a specific role in spermatogenesis (Dieterich et al, 2007;Kimmins et al, 2007;Tang et al, 2006) and oogenesis (Sharif et al, 2010), its physiological relevance in the regulation of mitosis is not well understood.…”

Aurora kinases and spindle assembly: Variations on a common theme?

“…AurC is expressed at high levels in the germ line cells, where it presumably plays an AurB-like role, as a catalytic subunit of the CPC. 24,[39][40][41] Despite the prominent role of the Aurora kinases in mitosis, the mechanisms that control their localization and activity are not well defined. Understanding these mechanisms is important, because Aurora kinases are frequently overexpressed in cancers and therefore considered candidate targets for tailored antineoplastic therapies.…”

Reduced ability to recover from spindle disruption and loss of kinetochore spindle assembly checkpoint proteins in oocytes from aged mice

“…To examine this idea further, we measured for changes, with respect to maternal age, in levels of 2 proteins: Mad2 and phosphorylated Aurora C (pAurora C). Aurora C is a substitute of Aurora B during meiosis, [34][35][36][37] and its active form pAurora C is thought to be involved in destabilizing erroneous KT-MT attachment, as such contributing to the fidelity of bivalent division. 34,[38][39][40] One further reason for examining Mad2 is that previous studies have shown that levels of this transcript, like those of other SAC components, are lower in oocytes of both aged mice and humans.…”