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Fig. 2 | Journal of Inflammation

Fig. 2

From: The functional characterization of phosphorylation of tristetraprolin at C-terminal NOT1-binding domain

Fig. 2

Ser316 phosphorylation decreases interaction with the CNOT1 complex and suppresses TTP activity. A Immunoprecipitation analysis. HEK293T cells were transfected with indicated Flag-TTP constructs and whole cell extracts were immunoprecipitated by anti-Flag. The precipitated protein complexes were analyzed by western blotting with antibodies against the CCR4-NOT complex as indicated. The asterisk indicates non-specific signals. B TTP directly interacts with CNOT1. HEK293T cells were transfected with siRNA specific for CNOT1, CNOT6, or CNOT7 or a negative-control siRNA (NC). After 24 h, cells were transfected again with the Flag-TTP plasmid. IP was performed with anti-Flag agarose and precipitated protein complexes were detected with antibodies against CNOT1, CNOT6, CNOT7, and Flag. C Immunoprecipitation analysis. HEK293T cells were transfected with indicated Flag-TTP constructs and whole cell extracts were immunoprecipitated by anti-Flag. The precipitated protein complexes were analyzed by western blotting with indicated antibodies. The asterisk indicates antibody heavy chain signals. D HEK293T cells were transfected with WT, S316A, or S52,178A Flag-TTP and treated with or without 1 μM of okadaic acid for 1 h. Whole cell extracts were immunoprecipitated with anti-Flag and western blotting with indicated antibodies. The asterisk indicates antibody heavy chain signals

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