1. ¹Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic
2. ²Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic

Correspondence: Professor T Obsil, Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, 12843 Prague, Czech Republic. E-mail: obsil@natur.cuni.cz

Abstract

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.