Journal
FEBS LETTERS
Volume 584, Issue 6, Pages 1111-1118Publisher
WILEY
DOI: 10.1016/j.febslet.2010.02.058
Keywords
Membrane; Protrusion; Invagination; EFC domain; F-BAR domain
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Science and Technology Corporation
- Ono Medical Research Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Takeda Science Foundation
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The extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation. Structured summary: MINT-7710892: EFCS pacsin2 (uniprotkb: Q9UNF0) and EFCS pacsin2 (uniprotkb: Q9UNF0) bind (MI: 0407) by X-ray crystallography (MI: 0114) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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