Cytosolic proteins can be modified cotranslationally by the installation of O-GlcNAc groups onto serine and threonine residues. This modification suppresses cotranslational ubiquitination and stabilizes proteins against proteasomal degradation.
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References
Balch, W.E., Morimoto, R.I., Dillin, A. & Kelly, J.W. Science 319, 916–919 (2008).
Zhu, Y. et al. Nat. Chem. Biol. doi:10.1038/nchembio.1774 (16 March 2015).
Sato, S., Ward, C.L. & Kopito, R.R. J. Biol. Chem. 273, 7189–7192 (1998).
Zhou, M., Fisher, E.A. & Ginsberg, H.N. J. Biol. Chem. 273, 24649–24653 (1998).
Bengtson, M.H. & Joazeiro, C.A. Nature 467, 470–473 (2010).
Duttler, S., Pechmann, S. & Frydman, J. Mol. Cell 50, 379–393 (2013).
Wang, F., Durfee, L.A. & Huibregtse, J.M. Mol. Cell 50, 368–378 (2013).
Hart, G.W., Housley, M.P. & Slawson, C. Nature 446, 1017–1022 (2007).
Zeidan, Q., Wang, Z., De Maio, A. & Hart, G.W. Mol. Biol. Cell 21, 1922–1936 (2010).
Hebert, D.N., Lamriben, L., Powers, E.T. & Kelly, J.W. Nat. Chem. Biol. 10, 902–910 (2014).
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Powers, E. An O-GlcNAc stamp of approval. Nat Chem Biol 11, 307–308 (2015). https://doi.org/10.1038/nchembio.1777
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DOI: https://doi.org/10.1038/nchembio.1777