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Q. Yan, J.–P. Liu, J. Qin, H. Feng, Y.–M. Xiao, W.–B. Liu, X.–Q. Huang, H.–G. Chen, Y. Liu, D.W. Li; Protein Phosphatase–1 Dephosphorylates Pax 6, A Major Transcription Factor In The Ocular Lens . Invest. Ophthalmol. Vis. Sci. 2006;47(13):2565.
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© ARVO (1962-2015); The Authors (2016-present)
Pax 6 is an evolutionarily conserved transcription factor and plays a critical role for the normal development of the eyes in human, mouse, zebrafish, and Drosophila. Previous studies have shown that Pax 6 is a phospho–protein and its phosphorylation by ERK and p38 greatly enhances its transactivation. Here, we present evidence to show that the protein phosphatase–1 dephosphorylates Pax–6 to modulate its function.
GST–Pax 6 fusion protein was generated and phosphorylated in vitro by p38 kinase. The phosphorylated Pax 6 was subjected to dephosphorylation by PP–1. Co–immunoprecipitation was used to determine the formation of Pax–6 and PP–1 complex.
Inhibition of PP–1 with protein phosphatase inhibitor enhances hyperphosphorylation of Pax 6. PP–1 can dephosphorylate Pax 6 in vitro. Pax 6 and PP–1 can form in vivo complex.
PP–1 may dephosphorylate Pax 6 to modulate its function in lens epithelial cells. Supported by EY 15765, Hormel Foundation, and the Lotus Scholar Professorship Funds from Hunan Province Government and Hunan Normal University.
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