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Sci. Signal., 29 March 2011
Vol. 4, Issue 166, p. ra19
[DOI: 10.1126/scisignal.2001556]


Editor's Summary

Losing Your Inhibitions
The antineoplastic drug cisplatin binds to actively replicating DNA, eliciting DNA lesions and, eventually, apoptosis. However, overexpression of the oncoprotein c-MYC can enable cancer cells to become resistant to cisplatin’s effects. Pyndiah et al. found that the c-MYC inhibitor BIN1 sensitized cells to DNA damage through a direct interaction with and inhibition of the DNA repair enzyme poly(ADP-ribose) polymerase 1 (PARP1). c-MYC, when overexpressed, inhibited expression of BIN1, thereby setting up a positive feedback loop for increased c-MYC activity and promoting cancer cell resistance to DNA-damaging agents like cisplatin.

Citation: S. Pyndiah, S. Tanida, K. M. Ahmed, E. K. Cassimere, C. Choe, D. Sakamuro, c-MYC Suppresses BIN1 to Release Poly(ADP-Ribose) Polymerase 1: A Mechanism by Which Cancer Cells Acquire Cisplatin Resistance. Sci. Signal. 4, ra19 (2011).

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Poly(ADP-ribose) polymerase 1 regulates nuclear reprogramming and promotes iPSC generation without c-Myc.
S.-H. Chiou, B.-H. Jiang, Y.-L. Yu, S.-J. Chou, P.-H. Tsai, W.-C. Chang, L.-K. Chen, L.-H. Chen, Y. Chien, and G.-Y. Chiou (2013)
J. Exp. Med. 210, 85-98
   Abstract »    Full Text »    PDF »
MYC, PARP1, and Chemoresistance: BIN There, Done That?.
S. Ganesan (2011)
Science Signaling 4, pe15
   Abstract »    Full Text »    PDF »

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