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Substrate selectivity of semisynthetic Akt with pSer473 or O-GlcNAcSer473

ABSTRACT: Akt is a Ser/Thr protein kinase that regulates cell growth, metabolism and is considered a therapeutic target for cancer. Regulation of Akt by membrane recruitment and post-translational modifications (PTMs) has been extensively studied. The most well-established mechanism for cellular Akt activation involves phosphorylation on its activation loop on Thr308 by PDK1 and on its C-terminal tail on Ser473 by mTORC2. Other C-terminal tail PTMs have been identified, but their functional impacts have not been well-characterized. We use expressed protein ligation (EPL) as a tool to produce semisynthetic Akt proteins to dissect the enzymatic functions of these PTMs. We performed kinase assays employing human protein microarrays to investigate global substrate specificity of Akt, comparing phosphorylated vs. O-GlcNAcylated Ser473 forms.

ORGANISM(S): synthetic construct Homo sapiens

PROVIDER: GSE181983 | GEO | 2021/08/13

REPOSITORIES: GEO

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Substrate selectivity for semisynthetic CK2 proteins with Pin1

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2011-10-24 | E-GEOD-33150 | biostudies-arrayexpress

Substrate selectivity for semisynthetic CK2 proteins with Pin1

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Expression data from control and Phospholipid dependent kinase 1 (PDK1) null cytotoxic T-lymphocytes (CTL) and from control and Akt inhibitor treated CTL

2011-02-01 | GSE26290 | GEO

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2011-02-01 | E-GEOD-26290 | biostudies-arrayexpress

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