PP2A is activated by cytochrome c upon formation of a diffuse encounter complex with SET/TAF-Iβ.

ABSTRACT: Intrinsic protein flexibility is of overwhelming relevance for intermolecular recognition and adaptability of highly dynamic ensemble of complexes, and the phenomenon is essential for the understanding of numerous biological processes. These conformational ensembles-encounter complexes-lack a unique organization, which prevents the determination of well-defined high resolution structures. This is the case for complexes involving the oncoprotein SET/template-activating factor-Iβ (SET/TAF-Iβ), a histone chaperone whose functions and interactions are significantly affected by its intrinsic structural plasticity. Besides its role in chromatin remodeling, SET/TAF-Iβ is an inhibitor of protein phosphatase 2A (PP2A), which is a key phosphatase counteracting transcription and signaling events cont

SUBMITTER: Casado-Combreras MA 

PROVIDER: S-EPMC9293736 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature