Ribosomal s6 kinase

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Some of the signalling events involving rsk.

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.

Substrates

Both p90 and p70 Rsk phosphorylate

cdc2.[1]

RSK phosphorylation of SOS1 (

Ras-MAPK pathway.[2]

p90rsk also regulates

c-Fos.[1]

Genomics

p90 Rsk-1 is located at 1p.[3]

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.[4]

p90 Rsk-3 is located at 6q27.[5]

Proteomics

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.[6]

Research history

Rsk was first identified in Xenopus laevis eggs by Erikson and Maller in 1985.[7]

References

  1. ^
    S2CID 42582996
    .
  2. PMID 22827337
    .
  3. ^ GenBank, Entrez Gene
  4. ^ Online Mendelian Inheritance in Man (OMIM): 300075
  5. PMID 7623830
    .
  6. ^ Based on figure 2 and 5 in Frödin and Gammeltoft, 1999.
  7. PMID 3856226
    .

External links
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