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Structure of a 14-3-3ε:FOXO3a^pS253 Phosphopeptide Complex Reveals 14-3-3 Isoform-Specific Binding of Forkhead Box Class O Transcription Factor (FOXO) Phosphoproteins.

ABSTRACT: The transcriptional activity of Forkhead Box O3 (FOXO3a) is inactivated by AKT-mediated phosphorylation on Serine 253 (S253), which enables FOXO3a binding to 14-3-3. Phosphorylated FOXO3a binding to 14-3-3 facilitates the nuclear exclusion of FOXO3a, causing cancer cell proliferation. The FOXO3a/14-3-3 interaction has, therefore, emerged as an important therapeutic target. Here, we report a comprehensive analysis using fluorescence polarization, isothermal titration calorimetry, small-angle X-ray scattering, X-ray crystallography, and molecular dynamics simulations to gain molecular-level insights into the interaction of FOXO3a^pS253 phosphopeptide with 14-3-3ε. A high-resolution structure of the fluorophore-labeled FOXO3a^pS253:14-3-3ε complex revealed a distinct mode

SUBMITTER: Mathivanan S

PROVIDER: S-EPMC9301721 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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Dataset Information

Structure of a 14-3-3ε:FOXO3a^pS253 Phosphopeptide Complex Reveals 14-3-3 Isoform-Specific Binding of Forkhead Box Class O Transcription Factor (FOXO) Phosphoproteins.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Structure of a 14-3-3ε:FOXO3apS253 Phosphopeptide Complex Reveals 14-3-3 Isoform-Specific Binding of Forkhead Box Class O Transcription Factor (FOXO) Phosphoproteins.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Structure of a 14-3-3ε:FOXO3a^pS253 Phosphopeptide Complex Reveals 14-3-3 Isoform-Specific Binding of Forkhead Box Class O Transcription Factor (FOXO) Phosphoproteins.