RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation.

doi:10.1074/jbc.M700906200

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Article

RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation.

The Journal of biological chemistry - 11 May 2007

Roux Philippe P, Shahbazian David, Vu Hieu, Holz Marina K, Cohen Michael S, Taunton Jack, Sonenberg Nahum, Blenis John

Abstract excerpt

Converging signals from the mammalian target of rapamycin (mTOR) and phosphoinositide 3-kinase (PI3K) pathways are well established to modulate translation initiation. Less is known regarding the molecular basis of protein synthesis regulated by other inputs, such as agonists of the Ras/extracellular signal-regulated kinase (ERK) signaling cascade. Ribosomal protein (rp) S6 is a component of the 40S ribosomal...

Topics

Cells, Cultured
HeLa Cells
Humans
Immunoblotting
Immunoprecipitation
Kidney
Luciferases
MAP Kinase Kinase Kinases
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phosphorylation

Polyribosomes

Protein Biosynthesis

RNA, Small Interfering

Ribosomal Protein S6

Ribosomal Protein S6 Kinases, 90-kDa

Ribosomes

Source

Open in PubMed Open full text

Identifiers

PMID: 17360704
DOI: 10.1074/jbc.M700906200
PMCID: PMC3618456

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