Open AccessRIOK2 phosphorylation by RSK promotes synthesis of the human small ribosomal subunit
Author(s) -
Emilie L. Cerezo,
Thibault Houlès,
Oriane Lié,
Marie-Kerguelen Sarthou,
Charlotte Audoynaud,
Geneviève Lavoie,
Maral Halladjian,
Sylvain Cantaloube,
Carine Froment,
Odile BurletSchiltz,
Y. Henry,
Philippe P. Roux,
Anthony K. Henras,
Yves Roméo
Publication year - 2021
Publication title -
plos genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.587
H-Index - 233
eISSN - 1553-7404
pISSN - 1553-7390
DOI - 10.1371/journal.pgen.1009583
Subject(s) - ribosome biogenesis , biology , microbiology and biotechnology , eukaryotic small ribosomal subunit , ribosomal s6 kinase , ribosomal protein , phosphorylation , mapk/erk pathway , ribosome , protein kinase a , eukaryotic ribosome , ribosomal protein s6 , biochemistry , protein phosphorylation , rna , p70 s6 kinase 1 , protein kinase b , gene
Ribosome biogenesis lies at the nexus of various signaling pathways coordinating protein synthesis with cell growth and proliferation. This process is regulated by well-described transcriptional mechanisms, but a growing body of evidence indicates that other levels of regulation exist. Here we show that the Ras/mitogen-activated protein kinase (MAPK) pathway stimulates post-transcriptional stages of human ribosome synthesis. We identify RIOK2, a pre-40S particle assembly factor, as a new target of the MAPK-activated kinase RSK. RIOK2 phosphorylation by RSK stimulates cytoplasmic maturation of late pre-40S particles, which is required for optimal protein synthesis and cell proliferation. RIOK2 phosphorylation facilitates its release from pre-40S particles and its nuclear re-import, prior to completion of small ribosomal subunits. Our results bring a detailed mechanistic link between the Ras/MAPK pathway and the maturation of human pre-40S particles, which opens a hitherto poorly explored area of ribosome biogenesis.