Interactomic affinity profiling by holdup assay: Acetylation and distal residues impact the PDZome-binding specificity of PTEN phosphatase
Fig 8
Changes in the PDZ binding profiles induced by changes in the PTEN peptides.
(A) Comparison between PTEN_11 (grey), PTEN_KR (light purple) and PTEN_Ac (dark blue) using a shared PDZ axis. For the wild-type PTEN_11 peptide, the PDZ domains were ranked in descending affinity order along the X-axis, from left to right according to the significant affinities for PTEN_11, and from right to left according to the significant affinities solely detected for PTEN_13. The remaining PDZ domains that bind only to the PTEN_KR peptide were added in the middle region. (B) Comparison between PTEN_11 (grey) and PTEN_13 (orange) on a shared PDZ axis. The PDZ domains were ranked along the X-axis in descending order, from left to right according to the significant affinities for PTEN_11, and from right to left according to the significant affinities exclusively detected for PTEN_13. The left and right regions thus show PDZ domains that prefer the shorter or the longer PTEN PBM version, respectively. The overall uncertainty on log(KD) values was estimated to be roughly ±0.12 in log(M) unit.