Serine 474 phosphorylation is essential for maximal Akt2 kinase activity in adipocytes.

ABSTRACT: The Ser/Thr protein kinase Akt regulates essential biological processes such as cell survival, growth, and metabolism. Upon growth factor stimulation, Akt is phosphorylated at Ser⁴⁷⁴; however, how this phosphorylation contributes to Akt activation remains controversial. Previous studies, which induced loss of Ser⁴⁷⁴ phosphorylation by ablating its upstream kinase mTORC2, have implicated Ser⁴⁷⁴ phosphorylation as a driver of Akt substrate specificity. Here we directly studied the role of Akt2 Ser⁴⁷⁴ phosphorylation in 3T3-L1 adipocytes by preventing Ser⁴⁷⁴ phosphorylation without perturbing mTORC2 activity. This was achieved by utilizing a chemical genetics approach, where ectopically expressed S474A Akt2 was engineered with a W80A muta

SUBMITTER: Kearney AL 

PROVIDER: S-EPMC6851323 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature