Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.

ABSTRACT: The multi-domain transcriptional coactivators CBP/p300 integrate a multitude of signaling inputs, interacting with more than 400 proteins via one or more of their globular domains. While CBP/p300 function is typically considered in terms of these structured domains, about half of the protein consists of intrinsically disordered regions (IDRs) of varying length. However, these IDRs have only been thought of as linkers that allow flexible spatial arrangement of the structured domains, but recent studies have shown that similar IDRs mediate specific and critical interactions in other proteins. To examine the roles of IDRs in CBP, we performed yeast-two-hybrid screenings of placenta and lung cancer cDNA libraries, which demonstrated that the long IDR linking the KIX domain and bromodomain of C

SUBMITTER: Contreras-Martos S 

PROVIDER: S-EPMC5498717 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature