Ribosomal Protein S6, a Target of Rapamycin, Is Involved in the Regulation of rRNA Genes by Possible Epigenetic Changes in Arabidopsis

Kim, Yun Kyoung; Kim, Sunghan; Shin, Yun Jeong; Hur, Yoon Sun; Kim, Woo Young; Lee, Myung Sok; Cheon, Choong Ill; Verma, Desh Pal S.

doi:10.1074/jbc.m113.515015

Cited by 67 publications

(54 citation statements)

References 44 publications

(41 reference statements)

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“…The RPS6 kinase of Arabidopsis, AtS6K1, is important in regulating cell division and growth (Henriques et al, 2010;Shin et al, 2012). New data suggest a non-ribosomal function of RPS6 in epigenetic regulation of rDNA transcription in Arabidopsis (Kim et al, 2014c). Further clarification will require mutational analyses to determine if RPS6 phosphorylation is biologically significant or simply a hallmark of S6K activity in plants.…”

Section: Ribosomal Protein Phosphorylationmentioning

confidence: 99%

“…An example of an extraribosomal function is the proposed role played by RPS6 in the regulation of transcription of rDNA and some RP gene transcripts in Arabidopsis (Kim et al, 2014c). This function involves direct interaction of non-phosphorylated RPS6 with Histone Deacetylase 2B (HD2B), which suppresses rDNA transcription.…”

Section: Ribosomal Protein Mutantsmentioning

confidence: 99%

“…It was hypothesized that phosphorylation of free RPS6 could reduce HD2B inhibition, thereby promoting rDNA transcription or processing. If regulated by TOR as proposed, this could place ribosome biogenesis and translational regulation under unified control (Kim et al, 2014c).…”

Section: Ribosomal Protein Mutantsmentioning

confidence: 99%

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Mechanism of Cytoplasmic mRNA Translation

Browning

Bailey‐Serres

2015

The Arabidopsis Book

186

220

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Protein synthesis is a fundamental process in gene expression that depends upon the abundance and accessibility of the mRNA transcript as well as the activity of many protein and RNA-protein complexes. Here we focus on the intricate mechanics of mRNA translation in the cytoplasm of higher plants. This chapter includes an inventory of the plant translational apparatus and a detailed review of the translational processes of initiation, elongation, and termination. The majority of mechanistic studies of cytoplasmic translation have been carried out in yeast and mammalian systems. The factors and mechanisms of translation are for the most part conserved across eukaryotes; however, some distinctions are known to exist in plants. A comprehensive understanding of the complex translational apparatus and its regulation in plants is warranted, as the modulation of protein production is critical to development, environmental plasticity and biomass yield in diverse ecosystems and agricultural settings.

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Section: Ribosomal Protein Phosphorylationmentioning

confidence: 99%

Section: Ribosomal Protein Mutantsmentioning

confidence: 99%

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Mechanism of Cytoplasmic mRNA Translation

Browning

Bailey‐Serres

2015

The Arabidopsis Book

186

220

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“…In our model of the b-arrestin/p70S6K complex, the orientation of the p70S6K makes it largely accessible to substrates and compatible with phosphorylation of the carboxyterminal regulatory sites on rpS6 within the ribosome (data not shown). Alternatively, extraribosomal location of rpS6 has been reported in Arabidopsis cell nuclei (81,82) as well as during premature 40S subunit assembly in the nucleolus (83). In addition to rpS6, nuclear location of b-arrestin 1 (84) and of p70S6K (48) has also been reported.…”

Section: Fsh-stimulated P70s6k Activity Within the B-arrestin Scaffolmentioning

confidence: 99%

G protein‐dependent signaling triggers a β‐arrestin‐scaffolded p70S6K/ rpS6 module that controls 5'TOP mRNA translation

et al. 2018

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Many interaction partners of b-arrestins intervene in the control of mRNA translation. However, how b-arrestins regulate this cellular process has been poorly explored. In this study, we show that b-arrestins constitutively assemble a p70S6K/ribosomal protein S6 (rpS6) complex in HEK293 cells and in primary Sertoli cells of the testis. We demonstrate that this interaction is direct, and experimentally validate the interaction interface between b-arrestin 1 and p70S6K predicted by our docking algorithm. Like most GPCRs, the biological function of folliclestimulating hormone receptor (FSHR) is transduced by G proteins and b-arrestins. Upon follicle-stimulating hormone (FSH) stimulation, activation of G protein-dependent signaling enhances p70S6K activity within the b-arrestin/p70S6K/rpS6 preassembled complex, which is not recruited to the FSHR. In agreement, FSH-induced rpS6 phosphorylation within the b-arrestin scaffold was decreased in cells depleted of Ga s . Integration of the cooperative action of b-arrestin and G proteins led to the translation of 59 oligopyrimidine track mRNA with high efficacy within minutes of FSH input. Hence, this work highlights new relationships between G proteins and b-arrestins when acting cooperatively on a common signaling pathway, contrasting with their previously shown parallel action on the ERK MAP kinase pathway. In addition, this study provides insights into how GPCR can exert trophic effects in the

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“…RPS6 phosphorylation by S6 kinase 1 (S6K1) can increase the translation of diverse proteins containing 5'-terminal oligopyrimidine tract (5'-TOP) mRNA, suggesting that RPS6 contributes to the control of ribosome biogenesis [7]. RPS6 was found to form a complex with a histone deacetylase AtHD2B and to bind to rDNA promoter in Arabidopsis [8]. Protoplasts overexpressing both RPS6 and AtHD2B respectively showed decrease in rDNA transcription.…”

Section: Introductionmentioning

confidence: 99%