In molecular biology, ribosomal s6 kinase (rsk) is a family of protein kinases involved in signal transduction. There are two subfamilies of rsk, p90rsk, also known as MAPK-activated protein kinase-1 (MAPKAP-K1), and p70rsk, also known as S6-H1 Kinase or simply S6 Kinase. There are three variants of p90rsk in humans, rsk 1-3. Rsks are serine/threonine kinases and are activated by the MAPK/ERK pathway. There are two known mammalian homologues of S6 Kinase: S6K1 and S6K2.
p90 Rsk-2 is located at Xp22.2 and contains 22 exons. Mutations in this gene have been associated with Coffin-Lowry syndrome, a disease characterised by severe psychomotor retardation and other developmental abnormalities.[3]
The main distinguishing feature between p90rsk and p70rsk is that the 90 kDa family contain two non-identical kinase domains, while the 70 kDa family contain only one kinase domain.
Domain structure of rsk. Numbers refer to amino acid residues of p90 rsk-1 from rat.[5]
Research history
Rsk was first identified in Xenopus laevis eggs by Erikson and Maller in 1985.[6]
References
^ ab Morten Frödin and Steen Gammeltoft. 1999. Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction. Molecular and Cellular Endocrinology151(1-2):Pages 65-77 (PMID 10411321doi:10.1016/S0303-7207(99)00061-1 DOI)
^ Y Zhao, C Bjørbaek, S Weremowicz, C C Morton, and D E Moller. 1993. RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation. Mol Cell Biol. 15(8):4353–4363.
^ Based on figure 2 and 5 in Frödin and Gammeltoft, 1999.
^ Eleanor Erikson and James L. Maller. 1985. A Protein Kinase from Xenopus Eggs Specific for Ribosomal Protein S6. PNAS82(3):742-746