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Cellular Localization and Characterization of Cytosolic Binding Partners for Gla Domain-containing Proteins PRRG4 and PRRG2 *

Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 288, Issue: 36, Page: 25908-25914
2013
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PRRG4 regulates mitochondrial function and promotes migratory behaviors of breast cancer cells through the Src-STAT3-POLG axis

Abstract Background Breast cancer is the leading cause of cancer death for women worldwide. Most of the breast cancer death are due to disease recurrence

Article Description

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. Background: PRRG proteins were cloned more than a decade ago, but their function is still not known. Results: Several novel protein-protein interactions for PRRG are identified by array screening and pulldown analysis. Conclusion: PRRG-initiated signaling events most likely depend on proteins with WW domains. Significance: The protein-protein interactions identified here may help to elucidate the roles of PRRG proteins in different physiological settings.

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