EFC/F-BARドメインの構造機能解析 : エンドサイトーシスにおける細胞膜陥入機構 [in Japanese] Structure-Function Analysis of the EFC/F-BAR Domain : Mechanism of Membrane Invagination in Endocytosis [in Japanese]
Access this Article
Search this Article
<I>Pombe</I> 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.
X-RAYS 50(2), 161-168, 2008-04-30
The Crystallographic Society of Japan