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| '''Crystal structure of the EFC domain of Cdc42-interacting protein 4'''
| | ===Crystal structure of the EFC domain of Cdc42-interacting protein 4=== |
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| ==Overview==
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| Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17512409}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17512409 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17512409}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rsgi]] | | [[Category: Rsgi]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:28:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:02:18 2008'' |
