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Beschreibung

Ribosomal protein S6 kinase beta-1 (UniProt: P23443, also known as EC 2.7.11.1, S6K-beta-1, S6K1, 70 kDa ribosomal protein S6 kinase 1, P70S6K1, p70-S6K 1, Ribosomal protein S6 kinase I, Serine/threonine-protein kinase 14A, p70 ribosomal S6 kinase alpha, p70 S6 kinase alpha, p70 S6K-alpha, p70 S6KA) is encoded by the RPS6KB1 (also known as STK14A) gene (Gene ID: 6198) in human. P70S6K1 is a serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth, and cell cycle progression. It regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Upon mitogenic stimulation, phosphorylation by mTORC1 leads to its activation following dissociation from the EIF3 complex. The active p70S6K1 then phosphorylates and activates several substrates in the pre-initiation complex. It is also shown to play a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, which results in the inhibition of mTORC2 and Akt1 signaling. The protein kinase domain of p70S6K1 is localized to amino acids 910352 and the autoinhibitory domain is localized to amino acids 424-525. The autoinhibitory domain blocks phosphorylation within the AGC-kinase C-terminal domain and the activation loop. It also contains a TOR signaling (TOS) motif (aa 28-32) that is essential for its activation by mTORC1. Five isoforms of p70S6K1 have been described that are produced by alternative splicing and alternative initiation.