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. 2012 Mar 1;8(3):e1002566. doi: 10.1371/journal.ppat.1002566

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Cai et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) The Aurora A-induced phosphorylation on Ser 215 and Ser 315 was critical for LANA-mediated ubiquitylation of p53. MEF cells were cotransfected with different combinations of HA-Ub, HA-p53 (WT, S215A, S315A or S215A/S315A), LANA-myc (WT or ΔSOCS) and Aurora A-myc (WT or KR) as indicated in the figure. At 36 hr post-transfection with additional 6 hr MG132 treatment before harvest, cell lysates were analyzed by immunoblotting with as indicated antibodies. (B) LANA upregulated Aurora A-mediated phosphorylation of p53. MEF cells were cotransfected p53-FLAG with either plasmid expressing shAurora A or shLuc in the presence or absence of LANA-myc as indicated in the figure. At 36 hr post-transfection with additional 6 hr MG132 treatment before harvest, cell lysates were analyzed by immunoblotting with specific antibodies. The knockdown efficiency of shRNA against Aurora A is shown at the bottom panel.