Fig. 6.
Fig. 6. Specific inhibition of βc association with 14-3-3ζ by a phosphorylated peptide encompassing the 579-592 region of βc. Lysates of HEK293T cells transfected with βc were precipitated with GST–14-3-3-sepharose in the absence or in the presence of various concentrations of chemically synthesized peptides. Two βc peptide sequences were used, CLGPPHSRSLPDILG in either the nonphosphorylated (A) or serine585-phosphorylated (B) form and CPLSLRSKPSPGPGP in either the nonphosphorylated (C) or serine-phosphorylated (D) form. The appropriate phosphorylated serine in each peptide is underlined. The experiment was performed on 7.5% SDS-PAGE under reducing conditions. The presence of βc in the immunoprecipitates was determined by Western blotting with anti-βc antibody (MoAb 1C1).

Specific inhibition of βc association with 14-3-3ζ by a phosphorylated peptide encompassing the 579-592 region of βc. Lysates of HEK293T cells transfected with βc were precipitated with GST–14-3-3-sepharose in the absence or in the presence of various concentrations of chemically synthesized peptides. Two βc peptide sequences were used, CLGPPHSRSLPDILG in either the nonphosphorylated (A) or serine585-phosphorylated (B) form and CPLSLRSKPSPGPGP in either the nonphosphorylated (C) or serine-phosphorylated (D) form. The appropriate phosphorylated serine in each peptide is underlined. The experiment was performed on 7.5% SDS-PAGE under reducing conditions. The presence of βc in the immunoprecipitates was determined by Western blotting with anti-βc antibody (MoAb 1C1).

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