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B56γ-PP2A mediates dephosphorylation of CREB and ATF1.

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posted on 13.08.2010, 01:36 authored by Naval P. Shanware, Lihong Zhan, John A. Hutchinson, Sang Hwa Kim, Leah M. Williams, Randal S. Tibbetts

(A) Okadaic acid (OA) sensitivity. HEK 293T cells were left untreated or exposed to 10 nM and 100 nM OA for 1 h. They were then subjected to IR for the indicated times. Cell extracts were prepared and analyzed by immunoblotting with α-CREB, α-pCREB-108/111/114 and α-pCREB-121 antibodies. (B) PP2Ac knockdown stimulates DNA damage-dependent CREB phosphorylation. HEK 293T cells expressing an shRNA targeting PP2Ac were compared to cells expressing a non-targeting shRNA construct. Cells were exposed to 10 Gy IR for 2 h and subjected to immunoblotting analysis with α-CREB, α-pCREB-108/111/114, α-pCREB-121 and α-PP2Ac antibodies. (C) B56γ knockdown stimulates DNA damage-dependent CREB phosphorylation. HEK 293T cells expressing an shRNA targeting B56γ were compared to cells expressing a non-targeting shRNA construct. Cells were exposed to 10 Gy IR for 1 h and subjected to immunoblotting analysis with α-CREB, α-pCREB-108/111/114, α-pCREB-121 and α-B56γ antibodies. (D) Effects of B56γ knockdown on ATF1 Ser-47/50/51 phosphorylation. HEK 293T cells were transiently transfected with control or B56γ siRNA and the levels of ATF1 Ser-47/50/51 phosphorylation assessed using α-pATF1-47/50/51 antibodies.

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