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Akt1 is dynamically modified with O‐GlcNAc following treatments with PUGNAc and insulin‐like growth factor‐1
Author(s) -
Gandy Johanna C.,
Rountree Abigail E.,
Bijur Gautam N.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.051
Subject(s) - akt1 , phosphorylation , chemistry , insulin like growth factor , growth factor , kinase , biochemistry , medicine , microbiology and biotechnology , protein kinase b , biology , receptor
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 ‐phenylcarbamate (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 Akt1 nuclear localization.