Ribosomal protein S6 kinase beta-1 is an enzyme that in humans is encoded by the RPS6KB1 gene.[1][2]
This gene encodes a member of the RSK (ribosomal s6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates several residues of the S6 ribosomal protein. The kinase activity of this protein leads to an increase in protein synthesis and cell proliferation. According to a May 2010 online news release by the Cincinnati Cancer Consortium with the Academic Health Center of the University of Cincinnati, inhibition of the S6K1 protein, or a lack of it, slows the production of adipose (fat) cells by disrupting and retarding the initial "commitment stage" of their formation. The study could have implications for the treatment of obesity.[3] Amplification of the region of DNA encoding this gene and overexpression of this kinase are seen in some breast cancer cell lines. Another pathway for which P70 has proposed involvement is in muscle lengthening and growing. An ongoing study at the Medical College of Wisconsin has demonstrated that P70 is phosphorolated by passive stretch in the soleus muscle. This may be one of many protein kinases involved in muscle building. Alternative translational start sites have been described and alternative transcriptional splice variants have been observed but have not been thoroughly characterized.[2]
P70-S6 Kinase 1 has been shown to interact with CSNK2B,[4] EIF3B,[5] COASY,[6] KIAA1303,[7][8][9][10] POLDIP3,[11] Mammalian target of rapamycin,[12][13][14][15][16][17][18][19][20][21][22][23] PPP2R2A,[24][25] RBX1[26] and Ubiquitin C.[26]
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