Work

Flexibility in the PP1:spinophilin holoenzyme

Year: 2010

Type: article

Abstract: Protein phosphatase 1 (PP1) interacts with ∼200 regulatory proteins to form holoenzymes, which target PP1 to specific locations and regulate its specificity. While it is known that many PP1 regulatory proteins are dynamic in the unbound state, much less is known about the residual flexibility after PP1 holoenzyme formation. Here, we have used small angle X-ray scattering to investigate the flexibility of the PP1:spinophilin holoenzyme in solution. Collectively, our data shows that the PP1:spinophilin holoenzyme is dynamic in solution, which allows for an increased capture radius of spinophilin and is likely important for its biological role.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2010.11.022

Authors: Michael J. Ragusa, Marc Allaire, Angus C. Nairn, Rebecca Page, Wolfgang Peti

Institutions: Brown University, Brookhaven National Laboratory, Yale University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Neurological Disorders and Stroke

Awards: G136441228, Training in Molecular and Cell Biology and Biochemistry, Structural and Functional Analysis of Signaling Proteins in Dendritic Spines, G8649025582