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Rewiring of RSK-PDZ Interactome by Linear Motif Phosphorylation.

Abstract：

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

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gógl G,Biri-Kovács B,Durbesson F,Jane P,Nomine Y,Kostmann C,Bilics V,Simon M,Reményi A,Vincentelli R,Trave G,Nyitray L

doi

10.1016/j.jmb.2019.01.038

subject

Has Abstract

pub_date

2019-03-15 00:00:00

pages

1234-1249

issue

6

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(19)30058-0

journal_volume

431

pub_type

杂志文章

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