Skip to main content

S6K1 is acetylated at lysine 516 in response to growth factor stimulation

Fenton, TR, Gwalter, J, Cramer, R, Gout, IT (2010) S6K1 is acetylated at lysine 516 in response to growth factor stimulation. Biochemical and Biophysical Research Communications, 398 (3). 400 - 405. ISSN 0006-291X. (doi:10.1016/j.bbrc.2010.06.081) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1016/j.bbrc.2010.06.081

Abstract

The 70 kDa ribosomal protein S6 kinase 1 (S6K1) plays important roles in the regulation of protein synthesis, cell growth and metabolism. S6K1 is activated by the phosphorylation of multiple serine and threonine residues in response to stimulation by a variety of growth factors and cytokines. In addition to phosphorylation, we have recently shown that S6K1 is also targeted by lysine acetylation. Here, using tandem mass spectrometry we have mapped acetylation of S6K1 to lysine 516, a site close to the C-terminus of the kinase that is highly conserved amongst vertebrate S6K1 orthologues. Using acetyl-specific K516 antibodies, we show that acetylation of endogenous S6K1 at this site is potently induced upon growth factor stimulation. Although S6K1 acetylation and phosphorylation are both induced by growth factor stimulation, these events appear to be functionally independent. Indeed, experiments using inhibitors of S6K1 activation and exposure of cells to various stresses indicate that S6K1 acetylation can occur in the absence of phosphorylation and vice versa. We propose that K516 acetylation may serve to modulate important kinase-independent functions of S6K1 in response to growth factor signalling. (C) 2010 Elsevier inc. All rights reserved.

Item Type: Article
DOI/Identification number: 10.1016/j.bbrc.2010.06.081
Uncontrolled keywords: S6 kinase, Acetylation, p300, Acetyltransferases, KINASE PATHWAY, CELL-GROWTH, IN-VITRO, PROTEIN, PHOSPHORYLATION, ACTIVATION, LOCALIZATION, P300, BETA, MICE
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Tim Fenton
Date Deposited: 19 Dec 2018 06:08 UTC
Last Modified: 29 May 2019 18:59 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/61520 (The current URI for this page, for reference purposes)
Fenton, TR: https://orcid.org/0000-0002-4737-8233
  • Depositors only (login required):