Author:
Jané Pau,Gógl Gergő,Kostmann Camille,Bich Goran,Girault Virginie,Caillet-Saguy Célia,Eberling Pascal,Vincentelli Renaud,Wolff Nicolas,Travé Gilles,Nominé Yves
Abstract
AbstractProtein domains often recognize short linear protein motifs composed of a core conserved consensus sequence surrounded by less critical, modulatory positions. Here we used an accurate experimental approach combining high-throughput holdup chromatographic assay and fluorescence polarization to measure quantitative binding affinity profiles of the PDZ domain-binding motif (PBM) of PTEN phosphatase towards the 266 known human PDZ domains. Inclusion of N-terminal flanking residues, acetylation or mutation of a lysine at a modulatory position significantly altered the PDZome-binding profile of the PTEN PBM. A specificity index is also introduced to quantify the specificity of a given PBM over the complete PDZome. Our results highlight the impact of modulatory residues and post-translational modifications on PBM interactomes and their specificity.
Publisher
Cold Spring Harbor Laboratory
Cited by
2 articles.
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