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J. Biol. Chem., Vol. 276, Issue 18, 14572-14580, May 4, 2001

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UVA Induces Ser³⁸¹ Phosphorylation of p90^RSK/MAPKAP-K1 via ERK and JNK Pathways^*

Yiguo Zhang, Shuping Zhong, Ziming Dong^§, Nanyue Chen, Ann M. Bode, Wei-ya Ma, and Zigang Dong^¶

From  The Hormel Institute, University of Minnesota, Austin, Minnesota 55912 and the ^§ Department of Pathophysiology, Henan Medical University, Zhengzhou 450052, Peoples Republic of China

UVA exposure plays an important role in the etiology of skin cancer. The family of p90-kDa ribosomal S6 kinases (p90^RSK/MAPKAP-K1) are activated via phosphorylation. In this study, results show that UVA-induced phosphorylation of p90^RSK at Ser³⁸¹ through ERKs and JNKs, but not p38 kinase pathways. We provide evidence that UVA-induced p90^RSK phosphorylation and kinase activity were time- and dose-dependent. Both PD98059 and a dominant negative mutant of ERK2 blocked ERKs and p90^RSK Ser³⁸¹ phosphorylation, as well as p90^RSK activity. A dominant negative mutant of p38 kinase blocked UVA-induced phosphorylation of p38 kinase, but had no effect on UVA-induced Ser³⁸¹ phosphorylation of p90^RSK or kinase activity. UVA-induced p90^RSK phosphorylation and kinase activity were markedly attenuated in JnK₁/ and JnK₂/ cells. A dominant negative mutant of JNK₁ inhibited UVA-induced JNKs and p90^RSK phosphorylation and kinase activity, but had no effect on ERKs phosphorylation. PD169316, a novel inhibitor of JNKs and p38 kinase, inhibited phosphorylation of p90^RSK, JNKs, and p38 kinase, but not ERKs. However, SB202190, a selective inhibitor of p38 kinase, had no effect on p90^RSK or JNKs phosphorylation. Significantly, ERKs and JNKs, but not p38 kinase, immunoprecipitated with p90^RSK when stimulated by UVA and p90^RSK was a substrate for ERK2 and JNK2, but not p38 kinase. These data indicate clearly that p90^RSK Ser³⁸¹ may be phosphorylated by activation of JNKs or ERKs, but not p38 kinase.

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