Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
| Autor: | David Barford, Patricia T.W. Cohen, Marie Pierre Egloff, Philip Cohen, Greg Moorhead, Deborah F. Johnson |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular animal structures Protein Conformation Protein subunit Molecular Sequence Data Sequence alignment Peptide Plasma protein binding Saccharomyces cerevisiae Biology Crystallography X-Ray General Biochemistry Genetics and Molecular Biology Catalysis Protein structure Protein Phosphatase 1 Phosphoprotein Phosphatases Serine Animals Amino Acid Sequence Amino Acids Phosphorylation Structural motif Muscle Skeletal Molecular Biology Peptide sequence Conserved Sequence chemistry.chemical_classification General Immunology and Microbiology General Neuroscience Protein phosphatase 1 chemistry Biochemistry Rabbits Peptides Sequence Alignment Protein Binding Research Article |
| Zdroj: | The EMBO journal. 16(8) |
| ISSN: | 0261-4189 |
| Popis: | 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 (G M ) that targets PP1c to glycogen particles in muscle. Here we report the structure, at 3.0 A resolution, of PP1c in complex with a 13 residue peptide (G M[63–75] ) of G M . The residues in G M[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 G M[63–75] peptide and the M 110[1–38] peptide (which mimics the myofibrillar targeting M 110 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text