RIOK2 phosphorylation by RSK promotes synthesis of the human small ribosomal subunit.

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.

Meeting report from the first European OddPols meeting: Toulouse 2018.

The eleventh international conference on transcription by RNA polymerases I, III, IV and V (the OddPols) was held from June 26th to June 29th 2018 at the Museum of Natural History of Toulouse, France and organized by Anthony Henras and Olivier Gadal. The scientific committee was composed of David Engelke, Joachim Griesenbeck, Ross Hannan, Deborah Johnson, Richard Maraia, Christoph Müller, Craig Pikaard, David Schneider and Ian Willis. The organizers are grateful to the "Centre de Biologie Intégrative de Toulouse", for support in the organization of the event. Participants from 13 different countries presented their newest exciting results during the scientific sessions and during extended conversation hours in the cosy atmosphere of the botanic garden of the Museum. Here we present the highlights of all oral presentations.

Maturation of pre-40S particles in yeast and humans.

The synthesis of ribosomal subunits in eukaryotes requires the interplay of numerous maturation and assembly factors (AFs) that intervene in the insertion of ribosomal proteins within pre-ribosomal particles, the ribosomal subunit precursors, as well as in pre-ribosomal RNA (rRNA) processing and folding. Here, we review the intricate nuclear and cytoplasmic maturation steps of pre-40S particles, the precursors to the small ribosomal subunits, in both yeast and human cells, with particular emphasis on the timing and mechanisms of AF association with and dissociation from pre-40S particles and the roles of these AFs in the maturation process. We highlight the particularly complex pre-rRNA processing pathway in human cells, compared to yeast, to generate the mature 18S rRNA. We discuss the information gained from the recently published cryo-electron microscopy atomic models of yeast and human pre-40S particles, as well as the checkpoint/quality control systems that seem to operate to probe functional sites within yeast cytoplasmic pre-40S particles. This article is categorized under: RNA Processing > rRNA Processing Translation > Ribosome Biogenesis.