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[Preprint]. 2023 May 23:2023.04.12.536585. Originally published 2023 Apr 12. [Version 2] doi: 10.1101/2023.04.12.536585

Figure 3. PKCβ leads to dual phosphorylation of internal sites in the helical domain, with selectivity for apo p110γ and p110γ-p84 over p110γ-p101.

Figure 3.

A. Putative phosphorylation sites mapped on the structure of p110γ (PDB: 7MEZ) and cartoon schematic. The regions are colored based on domain schematics featured in Fig 2A.

B. Raw MS spectra of the unphosphorylated and phosphorylated peptide for a region spanning 579–592 (RYESLKHPKAYPKL) and 593–607 (FSSVKWGQQEIVAKT). The putative phosphorylation sites in the sequence are shown in red, with the m/z theoretical (m/z t) and m/z experimental (m/z t) shown below each sequence.

C-E. Extracted traces and ratios of the intensity of extracted ion traces of different phosphorylation site peptides (Top to bottom: S594/S595 and S582) from (C) p110γ, (D) p110γ/p84 or (E) p110γ/p101 samples treated with increasing concentration of PKCβ according to the legend. The black traces in the ratio graphs are the intensity of the non-phosphorylated peptide, and the red traces in the ratio graphs are the intensity of the phosphorylated peptide.