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Publication : Cellular localization and characterization of cytosolic binding partners for Gla domain-containing proteins PRRG4 and PRRG2.

First Author  Yazicioglu MN Year  2013
Journal  J Biol Chem Volume  288
Issue  36 Pages  25908-25914
PubMed ID  23873930 Mgi Jnum  J:313845
Mgi Id  MGI:6204603 Doi  10.1074/jbc.M113.484683
Citation  Yazicioglu MN, et al. (2013) Cellular localization and characterization of cytosolic binding partners for Gla domain-containing proteins PRRG4 and PRRG2. J Biol Chem 288(36):25908-14
abstractText  The genes encoding a family of proteins termed proline-rich gamma-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 gamma-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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