4HMY

Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1

Summary for 4HMY

• Entry DOI: 10.2210/pdb4hmy/pdb
• Descriptor: AP-1 complex subunit gamma-1, AP-1 complex subunit beta-1, AP-1 complex subunit mu-1, ... (7 entities in total)
• Functional Keywords: protein transport, protein trafficking, arf1 gtpase activation, arf1 gtpase binding, trans-golgi membrane
• Biological source: Mus musculus (mouse); More
• Cellular location: Golgi apparatus: P22892 Q10567 P35585 Q96PC3 P84077
• Total number of polymer chains: 5
• Total formula weight: 221752.89

Authors

Ren, X.,Farias, G.G.,Canagarajah, B.J.,Bonifacino, J.S.,Hurley, J.H. (deposition date: 2012-10-18, release date: 2013-03-06, Last modification date: 2023-09-20)

Primary citation

Ren, X.,Farias, G.G.,Canagarajah, B.J.,Bonifacino, J.S.,Hurley, J.H.
Structural Basis for Recruitment and Activation of the AP-1 Clathrin Adaptor Complex by Arf1.
Cell(Cambridge,Mass.), 152:755-767, 2013

PubMed Abstract: 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 β1 subunit of one AP-1 complex, while the back side of Arf1 binds to the central part of the γ subunit trunk of a second AP-1 complex. A third Arf1 interaction site near the N terminus of the γ subunit is important for recruitment, but not activation. These observations lead to a model for the recruitment and activation of AP-1 by Arf1.

PubMed: 23415225
DOI: 10.1016/j.cell.2012.12.042

Experimental method

X-RAY DIFFRACTION (7 Å)