| First Author | Ren X | Year | 2013 |
| Journal | Cell | Volume | 152 |
| Issue | 4 | Pages | 755-67 |
| PubMed ID | 23415225 | Mgi Jnum | J:201285 |
| Mgi Id | MGI:5512930 | Doi | 10.1016/j.cell.2012.12.042 |
| Citation | Ren X, et al. (2013) Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. Cell 152(4):755-67 |
| abstractText | AP-1 is a clathrin adaptor complex that sorts cargo between the trans-Golgi network and endosomes. AP-1 recruitment to these compartments requires Arf1-GTP. The crystal structure of the tetrameric core of AP-1 in complex with Arf1-GTP, together with biochemical analyses, shows that Arf1 activates cargo binding by unlocking AP-1. Unlocking is driven by two molecules of Arf1 that bridge two copies of AP-1 at two interaction sites. The GTP-dependent switch I and II regions of Arf1 bind to the N terminus of the beta1 subunit of one AP-1 complex, while the back side of Arf1 binds to the central part of the gamma subunit trunk of a second AP-1 complex. A third Arf1 interaction site near the N terminus of the gamma subunit is important for recruitment, but not activation. These observations lead to a model for the recruitment and activation of AP-1 by Arf1. |
