Article
Regulation of Hsf4b nuclear translocation and transcription activity by phosphorylation at threonine 472.
Biochimica et biophysica acta - 1 Mar 2014
Zhang Jun, Ma Zengyi, Wang Jiyan, Li Shulian, Zhang Yaqin, Wang Yuelin, Wang Mingli, Feng Xiaoli, Liu Xiang, Liu Guangchao, Lou Qiang, Cui Xiukun, Ma Yuanfang, Dong Zheng, Hu Yan-Zhong
Abstract excerpt
Hsf4b, a key regulator of postnatal lens development, is subjected to posttranslational modifications including phosphorylation. However, the phosphorylation sites in Hsf4b and their biological effects on the transcription activity of Hsf4b are poorly understood. Here we examined 17 potential phosphorylation residues in Hsf4b with alanine-scanning assays and found that a T472A mutation diminished Hsf4b-mediated...
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