We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1.
- Authors
Egloff, Marie-Pierre; Johnson, Deborah F.; Moorhead, Greg; Cohen, Patricia T. W.; Cohen, Philip; Barford, David
- Abstract
The diverse forms of protein phosphatase 1 in vivo result from the association of its catalytic subunit (PP1c) with different regulatory subunits, one of which is the G-subunit (GM) that targets PP1c to glycogen particles in muscle. Here we report the structure, at 3.0 Å resolution, of PP1c in complex with a 13 residue peptide (GM[63–75]) of GM. The residues in GM[63–75] that interact with PP1c are those in the Arg/Lys–Val/Ile–Xaa–Phe motif that is present in almost every other identified mammalian PP1-binding subunit. Disrupting this motif in the GM[63–75] peptide and the M110[1–38] peptide (which mimics the myofibrillar targeting M110 subunit in stimulating the dephosphorylation of myosin) prevents these peptides from interacting with PP1. A short peptide from the PP1-binding protein p53BP2 that contains the RVXF motif also interacts with PP1c. These findings identify a recognition site on PP1c, invariant from yeast to humans, for a critical structural motif on regulatory subunits. This explains why the binding of PP1 to its regulatory subunits is mutually exclusive, and suggests a novel approach for identifying the functions of PP1-binding proteins whose roles are unknown.
- Subjects
PHOSPHOPROTEIN phosphatases; GLYCOGEN; PEPTIDES; CARRIER proteins; YEAST
- Publication
EMBO Journal, 1997, Vol 16, Issue 8, p1876
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/16.8.1876