Journal
FEBS LETTERS
Volume 580, Issue 13, Pages 3051-3058Publisher
WILEY
DOI: 10.1016/j.febslet.2006.04.051
Keywords
Akt1; O-GlcNAc; PUGNAc; IGF-1; wheat germ agglutinin; GSK3 beta
Funding
- NINDS NIH HHS [R01 NS044853, R01 NS044853-04, NS044853] Funding Source: Medline
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The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473. In the present study, Akt1 was found to be constitutively modified with O-GlcNAc. Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels. Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation. PUGNAc treatment did not attenuate IGF-1 induced Akt1 phosphorylation. These results indicate that Akt1 can be simultaneously modified with O-GlcNAc and phosphorylated. However, PUGNAc induced the nuclear accumulation of Akt1 suggesting that the O-GlcNAc-modification on Akt1 may play a role in AktI nuclear localization. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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