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Structure/function relationships underlying regulation of FOXO transcription factors

T Obsil, V Obsilova

. 2008 ; 27 (16) : 2263-2275.

Language English Country Great Britain

Document type Review

E-resources

NLK ProQuest Central from 2000-01-01 to 1 year ago
Open Access Digital Library from 1997-01-01
Medline Complete (EBSCOhost) from 1997-01-09 to 2015-11-26
Health & Medicine (ProQuest) from 2000-01-01 to 1 year ago
Public Health Database (ProQuest) from 2000-01-01 to 1 year ago

The FOXO subgroup of forkhead transcription factors plays a central role in cell-cycle control, differentiation, metabolism control, stress response and apoptosis. Therefore, the function of these important molecules is tightly controlled by a wide range of protein-protein interactions and posttranslational modifications including phosphorylation, acetylation and ubiquitination. The mechanisms by which these processes regulate FOXO activity are mostly elusive. This review focuses on recent advances in structural studies of forkhead transcription factors and the insights they provide into the mechanism of DNA recognition. On the basis of these data, we discuss structural aspects of protein-protein interactions and posttranslational modifications that target the forkhead domain and the nuclear localization signal of FOXO proteins.

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$a The FOXO subgroup of forkhead transcription factors plays a central role in cell-cycle control, differentiation, metabolism control, stress response and apoptosis. Therefore, the function of these important molecules is tightly controlled by a wide range of protein-protein interactions and posttranslational modifications including phosphorylation, acetylation and ubiquitination. The mechanisms by which these processes regulate FOXO activity are mostly elusive. This review focuses on recent advances in structural studies of forkhead transcription factors and the insights they provide into the mechanism of DNA recognition. On the basis of these data, we discuss structural aspects of protein-protein interactions and posttranslational modifications that target the forkhead domain and the nuclear localization signal of FOXO proteins.
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