Phospho-RSK1 p90 (T573) Recombinant Rabbit Monoclonal Antibody [JE50-12]

Function

The family of ribosomal S6 kinases (Rsks), designated Rsk-1, Rsk-2 and Rsk-3, are important signaling intermediates that mediate responses to a broad range of ligand-activated receptor tyrosine kinases. It has been established that Rsk-3 is not activated by MAP kinase in vitro, unlike Rsk-1 and Rsk-2. A unique feature common to the three members of the Rsk family is that each possesses two non-identical complete kinase catalytic domains. The Rsk family amino-terminal kinase domain is phosphorylated on Ser 227 by 3-phosphoinositide-dependent protein kinase-1 (PDK1), which increases the kinase activity of Rsk. In the carboxy-terminal kinase domain, Rsk-1 and Rsk-2 are autophosphorylated on Ser 380 and Ser 386, respectively, which mediates the docking of PDK1 to Rsk in order to promote phosphorylation of substrates, such as histone H3.

Background References

1. Smadja-Lamère N et al. Insulin Activates RSK (p90 Ribosomal S6 Kinase) to Trigger a New Negative Feedback Loop That Regulates Insulin Signaling for Glucose Metabolism. J Biol Chem 288:31165-76 (2013).

2. Tangredi MM et al. The C-terminal kinase and ERK-binding domains of Drosophila S6KII (RSK) are required for phosphorylation of the protein and modulation of circadian behavior. J Biol Chem 287:16748-58 (2012).

Sequence Similarity

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.

Post-translational Modification

Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-380, as part of the activation process. May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.; N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

Subcellular Location

Nucleus, Cytoplasm.

UNIPROT

SwissProt: Q15418 Human

SwissProt: P18653 Mouse

SwissProt: Q63531 Rat

Synonyms