Architectures of membrane deformation complexes. Depicted are, from top, atomic level structures, schematics for the molecular architectures of subunit assemblies, architecture of the coats lattice, and depictions of how these complexes may assemble at the membrane. In all cases, α-structures are shown in pink and β-structures in blue. For complex assemblies at the membrane, the deformation subunits are shown in red and blue, and associated factors responsible for cargo recognition or other interactions are in gray. Note that the topology of membrane deformation between protocoatomer and most BAR domain complexes is 180° out of phase with the ESCRT complex. The figure incorporates ribbon diagrams for the crystallographic structures of the Nup145c/Sec13 dimer (PDB: 3jro; Brohawn and Schwartz, 2009); Sec13/31 dimer (PDB: 2pm6 and 2pm9; Fath et al., 2007); the N-terminal β-propeller domain of human Nup133 (PDB: 1xks; 75–482; Berke et al., 2004) and the human C-terminal helical domain (PDB: 3i4r; 517–1156; Whittle and Schwartz, 2009); two BAR domain homodimers, human formin-binding protein 17 (PDB: 2efl; 1–300; Shimada et al., 2007) and human PACSIN2/Syndapin II (PDB: 3abh; 16–304); the tetrameric ESCRT III complex (PDB: 2zme) consisting of vacuolar-sorting protein SNF8 (34–250), two copies of vps36 (172–386), and one copy of vps25 (4–103); the clathrin heavy chain, based on the structure of a bovine C-terminal helical region (PDB: 3lvh; 1077–1630; Wilbur et al., 2010) and the rat N-terminal region (PDB: 1bpo; 1–494; ter Haar et al., 1998); and finally a portion of the yeast COPI coat (PDB: 3mkq; β subunits 1–814; β subunits 624–818; Lee and Goldberg, 2010). Note the reverse topology of BAR domain complexes is omitted for clarity.