Ontology highlight
ABSTRACT:
SUBMITTER: Follis AV
PROVIDER: S-EPMC5899648 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Follis Ariele Viacava AV Llambi Fabien F Kalkavan Halime H Yao Yong Y Phillips Aaron H AH Park Cheon-Gil CG Marassi Francesca M FM Green Douglas R DR Kriwacki Richard W RW
Nature chemical biology 20180305 5
Intrinsically disordered regions (IDRs) of proteins often regulate function upon post-translational modification (PTM) through interactions with folded domains. An IDR linking two α-helices (α1-α2) of the antiapoptotic protein Bcl-xL experiences several PTMs that reduce antiapoptotic activity. Here, we report that PTMs within the α1-α2 IDR promote its interaction with the folded core of Bcl-xL that inhibits the proapoptotic activity of two types of regulatory targets, BH3-only proteins and p53. ...[more]