AI Article Synopsis
- Researchers have identified and studied proline-rich γ-carboxyglutamic acid (PRRG) proteins, but their functions are still unclear.
- They discovered PRRG4's interactions with other proteins using WW domain arrays, revealing new protein-protein connections.
- The study also identified a critical WW binding motif in PRRG4, suggesting that PRRG proteins may play important roles in various physiological processes.
Article Abstract
The genes encoding a family of proteins termed proline-rich γ-carboxyglutamic acid (PRRG) proteins were identified and characterized more than a decade ago, but their functions remain unknown. These novel membrane proteins have an extracellular γ-carboxyglutamic acid (Gla) protein domain and cytosolic WW binding motifs. We screened WW domain arrays for cytosolic binding partners for PRRG4 and identified novel protein-protein interactions for the protein. We also uncovered a new WW binding motif in PRRG4 that is essential for these newly found protein-protein interactions. Several of the PRRG-interacting proteins we identified are essential for a variety of physiologic processes. Our findings indicate possible novel and previously unidentified functions for PRRG proteins.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3764795 | PMC |
| http://dx.doi.org/10.1074/jbc.M113.484683 | DOI Listing |
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