Ribosomal Protein S6 Phosphorylation: Four Decades of Research

Oded Meyuhas*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

207 Scopus citations

Abstract

The phosphorylation of ribosomal protein S6 (rpS6) has been described for the first time about four decades ago. Since then, numerous studies have shown that this modification occurs in response to a wide variety of stimuli on five evolutionarily conserved serine residues. However, despite a large body of information on the respective kinases and the signal transduction pathways, the physiological role of rpS6 phosphorylation remained obscure until genetic manipulations were applied in both yeast and mammals in an attempt to block this modification. Thus, studies based on both mice and cultured cells subjected to disruption of the genes encoding rpS6 and the respective kinases, as well as the substitution of the phosphorylatable serine residues in rpS6, have laid the ground for the elucidation of the multiple roles of this protein and its posttranslational modification. This review focuses primarily on newly identified kinases that phosphorylate rpS6, pathways that transduce various signals into rpS6 phosphorylation, and the recently established physiological functions of this modification. It should be noted, however, that despite the significant progress made in the last decade, the molecular mechanism(s) underlying the diverse effects of rpS6 phosphorylation on cellular and organismal physiology are still poorly understood.

Original languageEnglish
Title of host publicationInternational Review of Cell and Molecular Biology, 2015
EditorsKwang W. Jeon
PublisherElsevier Inc.
Pages41-73
Number of pages33
ISBN (Print)9780128022771
DOIs
StatePublished - 2015

Publication series

NameInternational Review of Cell and Molecular Biology
Volume320
ISSN (Print)1937-6448

Keywords

  • Cell proliferation
  • Cell size
  • Glucose homeostasis
  • MTOR
  • Protein synthesis
  • Ribosomal protein S6
  • RSK
  • S6 kinase
  • Tumorigenicity

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