Journal
CELL
Volume 152, Issue 4, Pages 755-767Publisher
CELL PRESS
DOI: 10.1016/j.cell.2012.12.042
Keywords
-
Categories
Funding
- U. S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- NICHD
- NIDDK, NIH
Ask authors/readers for more resources
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 beta 1 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available