Rewiring of RSK-PDZ Interactome by Linear Motif Phosphorylation.
作者： Gergő Gógl , Beáta Biri-Kovács , Fabien Durbesson , Pau Jane , Yves Nomine
DOI: 10.1016/J.JMB.2019.01.038
关键词:
摘要: Phosphorylation of short linear peptide motifs is a widespread process for the dynamic regulation protein-protein interactions. However, global impact phosphorylation events on interactome rarely addressed. The disordered C-terminal tail ribosomal S6 kinase 1 (RSK1) binds to PDZ domain-containing scaffold proteins, and it harbors phosphorylatable PDZ-binding motif (PBM) responsive epidermal growth factor stimulation. Here, we examined binding two versions RSK1 PBM, either phosphorylated or unphosphorylated at position -3, almost all (95%) 266 domains human proteome. PBM dramatically altered domain-binding landscape RSK1, by strengthening weakening numerous interactions various degrees. RSK-PDZome analyzed in this study reveals how motif-based phospho-switches convey stimulus-dependent changes context related network components.
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