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M110164200v1
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Papers In Press, published online ahead of print March 4, 2002
J. Biol. Chem, 10.1074/jbc.M110164200
Submitted on October 22, 2001
Revised on February 26, 2002
Accepted on March 4, 2002

Ultraviolet light inhibits translation through activation of the unfolded protein response kinase PERK in the lumen of the endoplasmic reticulum

Shiyong Wu, Yuanyuan Hu, Ju-lin Wang, Madhumita Chatterjee, Yuguang Shi, and Randal J. Kaufman

Radiation Oncology, University of Michigan Medical School, Ann Arbor, MI 48109

Corresponding Author: shiyongw{at}umich.edu

Exposure to ultraviolet light can cause inflammation, premature skin aging and cancer. UV-irradiation alters the expression of multiple genes that encode functions to repair DNA-damage, arrest cell growth and induce apoptosis. In addition, UV-irradiation inhibits protein synthesis, although the mechanism is not known. In this report, we show that UV-irradiation induces phosphorylation of eukaryotic translation initiation factor 2 on the alpha subunit (eIF2a) and inhibits protein synthesis in a dosage- and time- dependent manner. The UV-induced phosphorylation of eIF2a was prevented by the over-expression of a non-phosphorylatable mutant of eIF2a (S51A). PERK is an eIF2a protein kinase localized to the endoplasmic reticulum that is activated by the accumulation of unfolded proteins in the ER. Expression of trans-dominant-negative mutants of PERK also prevented eIF2a phosphorylation upon UV treatment and protected from the associated translation attenuation. The lumenal domain of dominant-negative mutant PERK formed heterodimers with endogenous PERK to inhibit the PERK signaling pathway. In contrast, eIF2a phosphorylation was not inhibited by over-expression of a trans-dominant-negative mutant PKR, supporting that UV-induced eIF2a phosphorylation is specifically mediated by PERK. These results support a novel mechanism by which UV-irradiation regulates translation via an ER-stress signaling pathway.


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