Evidence toward a dual phosphatase mechanism that restricts Aurora A (Thr-295) phosphorylation during the early embryonic cell cycle
Q Kang, J Srividhya, J Ipe, JR Pomerening - Journal of Biological Chemistry, 2014 - ASBMB
The mitotic kinase Aurora A (AurA) is regulated by a complex network of factors that includes
co-activator binding, autophosphorylation, and dephosphorylation. Dephosphorylation of
AurA by PP2A (human, Ser-51; Xenopus, Ser-53) destabilizes the protein, whereas mitotic
dephosphorylation of its T-loop (human, Thr-288; Xenopus, Thr-295) by PP6 represses AurA
activity. However, AurA (Thr-295) phosphorylation is restricted throughout the early
embryonic cell cycle, not just during M-phase, and how Thr-295 is kept dephosphorylated …
co-activator binding, autophosphorylation, and dephosphorylation. Dephosphorylation of
AurA by PP2A (human, Ser-51; Xenopus, Ser-53) destabilizes the protein, whereas mitotic
dephosphorylation of its T-loop (human, Thr-288; Xenopus, Thr-295) by PP6 represses AurA
activity. However, AurA (Thr-295) phosphorylation is restricted throughout the early
embryonic cell cycle, not just during M-phase, and how Thr-295 is kept dephosphorylated …
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