| First Author | Duric I | Year | 2025 |
| Journal | Biochem Biophys Res Commun | Volume | 749 |
| Pages | 151337 | PubMed ID | 39837222 |
| Mgi Jnum | J:372452 | Mgi Id | MGI:7867006 |
| Doi | 10.1016/j.bbrc.2025.151337 | Citation | Duric I, et al. (2025) WBP1L, a transmembrane adaptor protein involved in the regulation of hematopoiesis, is controlled by CRL1(beta-TrCP) ubiquitin ligases. Biochem Biophys Res Commun 749:151337 |
| abstractText | WBP1L is a broadly expressed transmembrane adaptor protein involved in regulating hematopoietic stem cell function and T cell development. It interacts with NEDD4-family E3 ubiquitin ligases and regulates important chemokine receptor CXCR4. Using tandem affinity purification coupled with mass spectrometry, we identified novel WBP1L interactions with the IFNgamma receptor and the Cullin-RING ubiquitin ligases CRL1(beta-TrCP1/2). We found that WBP1L interaction with the IFNgamma receptor serves to downregulate proximal IFNgamma receptor signaling in female macrophages, while the interaction with CRL1(beta-TrCP1/2) ubiquitin ligases regulates WBP1L protein levels. Disrupting this interaction, as well as inhibiting proteasome activity or neddylation, increased WBP1L protein levels, demonstrating that CRL1(beta-TrCP1/2) ubiquitin ligases regulate WBP1L protein abundance. These data provide important insights into the mechanisms controlling WBP1L function. |
