| First Author | Nakamura T | Year | 2008 |
| Journal | Genes Dev | Volume | 22 |
| Issue | 9 | Pages | 1244-56 |
| PubMed ID | 18451111 | Mgi Jnum | J:134653 |
| Mgi Id | MGI:3789451 | Doi | 10.1101/gad.1632308 |
| Citation | Nakamura T, et al. (2008) PX-RICS mediates ER-to-Golgi transport of the N-cadherin/beta-catenin complex. Genes Dev 22(9):1244-56 |
| abstractText | Cadherins mediate Ca2+-dependent cell-cell adhesion. Efficient export of cadherins from the endoplasmic reticulum (ER) is known to require complex formation with beta-catenin. However, the molecular mechanisms underlying this requirement remain elusive. Here we show that PX-RICS, a beta-catenin-interacting GTPase-activating protein (GAP) for Cdc42, mediates ER-to-Golgi transport of the N-cadherin/beta-catenin complex. Knockdown of PX-RICS expression induced the accumulation of the N-cadherin/beta-catenin complex in the ER and ER exit site, resulting in a decrease in cell-cell adhesion. PX-RICS was also required for ER-to-Golgi transport of the fibroblast growth factor-receptor 4 (FGFR4) associated with N-cadherin. PX-RICS-mediated ER-to-Golgi transport was dependent on its interaction with beta-catenin, phosphatidylinositol-4-phosphate (PI4P), Cdc42, and its novel binding partner gamma-aminobutyric acid type A receptor-associated protein (GABARAP). These results suggest that PX-RICS ensures the efficient entry of the N-cadherin/beta-catenin complex into the secretory pathway, and thereby regulates the amount of N-cadherin available for cell adhesion and FGFR4-mediated signaling. |
