Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

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

RESEARCH ARTICLES

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).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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 »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882