FIGURE 2:

Structural determinants of ARF association with membranes and interactors. ARFs have four regions that change conformation between GDP- and GTP-bound forms: the canonical switch 1 (in orange) and switch 2 (in magenta) that directly sense the nature of the bound nucleotide; the myristoylated N-terminal helix (in blue), which is autoinhibitory in ARF-GDP and binds the membrane in ARF-GTP; and the interswitch (in red) that functions as a push button to ensure allosteric communication between the membrane- and the nucleotide-binding sites. GEFs, GAPs, and effectors generally bind to switch 1, switch 2, and/or the interswitch by one domain (in light yellow) and carry other domains that bind to the membrane (in light blue). The membrane bilayer is denoted in gray.