How an intrinsically disordered regulatory subunit assembles a PP1:eIF2 complex
Alexander C. Jones,
Jian Wu,
Susan S. Taylor
Affiliations
Alexander C. Jones
Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA
Jian Wu
Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA
Susan S. Taylor
Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA; Corresponding author
Fatalska et al.1 use an interdisciplinary strategy to elucidate how an intrinsically disordered regulatory subunit of protein phosphatase 1 binds trimeric eIF2 and positions the phosphatase-substrate complex for dephosphorylation. As validation, they show that a disease mutation abolishes the interaction.
