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Article

Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.

Molecular and cellular biology - 1 Jul 2003

Roux Philippe P, Richards Stephanie A, Blenis John

Abstract excerpt

Stimulation of the Ras/extracellular signal-regulated kinase (ERK) pathway can modulate cell growth, proliferation, survival, and motility. The p90 ribosomal S6 kinases (RSKs) comprise a family of serine/threonine kinases that lie at the terminus of the ERK pathway. Efficient RSK activation by ERK requires its interaction through a docking site located near the C terminus of RSK, but the regulation of this...

Topics

Amino Acid Sequence
Binding Sites
Cells, Cultured
Epidermal Growth Factor
Extracellular Matrix
Humans
Isoenzymes
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3
Mitogen-Activated Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mitogens

Molecular Sequence Data

Mutation

Phosphorylation

Protein Kinases

Protein Structure, Tertiary

Ribosomal Protein S6 Kinases

Ribosomal Protein S6 Kinases, 90-kDa

Source

Open in PubMed Open full text

Identifiers

PMID: 12832467
DOI: 10.1128/MCB.23.14.4796-4804.2003
PMCID: PMC162206

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Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.PMID 12832467Read ↗

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