Abstract
Pombe Cdc 15 homology (PCH) proteins are involved in a variety of actin-based processes, including clathrin-mediated endocytosis. The PCH proteins contain an evolutionarily conserved, EFC/F-BAR domain for membrane association and tubulation. We solved the crystal structures of the EFC domains of human FBP 17 and CIP4. The structures revealed a gently-curved helicalbundle dimer, which forms filaments through end-to-end interactions in the crystals. The structural and biochemical data suggested a mechanistic model, in which the curved EFC filament drives tubulation. The electron micrographs of the EFC-induced tubular membranes supported this model. The physiological role of the EFC domain in clathrin-mediated endocytosis is discussed.
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