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Function of WW domains as phosphoserine- or phosphothreonine-binding modules.
1Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.
Science (New York, N.Y.)
|February 26, 1999
Summary
Researchers discovered that WW domains, specifically the Pin1 WW domain, act as phosphoserine- or phosphothreonine-binding modules. This binding is crucial for protein interactions and Pin1
Area of Science:
- Molecular Biology
- Cell Signaling
- Protein Biochemistry
Background:
- Protein-interacting modules dictate signal transduction specificity.
- Phosphorylation regulates the assembly of signaling complexes.
- Phosphotyrosine-binding modules are known, but phosphoserine/threonine-binding modules are undescribed.
Purpose of the Study:
- To characterize the binding properties of WW domains.
- To investigate the role of WW domains in protein-protein interactions and signaling.
- To determine if WW domains can bind phosphoserine or phosphothreonine residues.
Main Methods:
- Studied WW domains from Pin1 and Nedd4.
- Assessed binding to phosphoproteins in a phosphorylation-dependent manner.
- Investigated the functional requirement of phosphoserine/threonine-binding for Pin1 activity in vitro and in vivo.
Main Results:
- WW domains of Pin1 and Nedd4 bind phosphoproteins, including enzyme substrates.
- The Pin1 WW domain functions as a phosphoserine/phosphothreonine-binding module.
- This binding activity is essential for Pin1's substrate interaction and in vivo function.
Conclusions:
- WW domains represent a novel class of phosphoserine/threonine-binding modules.
- Pin1's WW domain is critical for its biological role through specific phosphoprotein recognition.
- This finding expands the understanding of signaling complex regulation via phosphorylation-dependent interactions.
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