PMID: 18196973Jan 17, 2008Paper

c-MYC protein is degraded in response to UV irradiation

Cell Cycle
Sébastien BrittonPatrick Calsou

Abstract

The c-MYC proto-oncogene encodes a transcription factor that is critical for cell growth and proliferation. It is one of the genes frequently altered in cancer cells in which it exhibits constitutive activity. The half-life of c-MYC is very short in quiescent cells due to ubiquitin-mediated proteolysis. We report here the rapid and dose-dependent decline of c-MYC protein level after UV-irradiation in various human and rodent cells. This decline is due to a proteasomal degradation of c-MYC protein and does not require the binding sites for the FBW7 and SKP2 ubiquitin ligases. Together, our data exclude a prominent role for the stress-responsive kinase PAK2, for the major phosphoinositide 3-kinase related protein kinases ATR, ATM, DNA-PK and mTOR and for ERK, JNK and p38 mitogen activated protein kinases in this UV-induced degradation process. We propose that c-MYC degradation is part of the global cell response to UV-damage, complementary to the accumulation and activation of the p53 transcription factor. By contributing to the replication arrest after infliction of lesions to the genome, the induced degradation of c-MYC may be part of the safeguard mechanisms maintaining genome stability.

Citations

Aug 15, 2013·Archives of Dermatological Research·Jee-Youn KimSun Lee
May 23, 2009·Nature Reviews. Cancer·Steffi HeroldMartin Eilers
Mar 10, 2010·Proceedings of the National Academy of Sciences of the United States of America·Ian G CannellMartin Bushell
Aug 14, 2008·The Journal of Biological Chemistry·Melissa PopowskiCarla L Van Den Berg
Oct 5, 2012·Molecular Biology of the Cell·Zengpeng LiSi Qing Zhang
Aug 3, 2011·Molecular and Cellular Biology·Kishore B ChallagundlaMu-Shui Dai
Jun 6, 2014·Oncotarget·Lixia WangZhiwei Wang
Aug 11, 2021·Journal of Hematology & Oncology·Seyed Esmaeil AhmadiMajid Safa

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