| Literature DB >> 30661852 |
Ewald Heroes1, Gerd Van der Hoeven2, Meng S Choy3, Javier Del Pino Garcia2, Mónica Ferreira2, Mieke Nys4, Rita Derua5, Monique Beullens2, Chris Ulens4, Wolfgang Peti3, Luc Van Meervelt6, Rebecca Page7, Mathieu Bollen8.
Abstract
SDS22 is an ancient regulator of protein phosphatase-1 (PP1). Our crystal structure of SDS22 shows that its twelve leucine-rich repeats adopt a banana-shaped fold that is shielded from solvent by capping domains at its extremities. Subsequent modeling and biochemical studies revealed that the concave side of SDS22 likely interacts with PP1 helices α5 and α6, which are distal from the binding sites of many previously described PP1 interactors. Accordingly, we found that SDS22 acts as a "third" subunit of multiple PP1 holoenzymes. The crystal structure of SDS22 also revealed a large basic surface patch that enables binding of a phosphorylated form of splicing factor BCLAF1. Taken together, our data provide insights into the formation of PP1:SDS22 and the recruitment of additional interaction proteins, such as BCLAF1.Entities:
Keywords: BCLAF1; MYPT1; PNUTS; RepoMan; SDS22; THRAP3; leucine-rich repeats; protein dephosphorylation; protein phosphatase-1
Year: 2019 PMID： 30661852 PMCID： PMC6538287 DOI： 10.1016/j.str.2018.12.002
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006