| Literature DB >> 20188097 |
Atsushi Shimada1, Kazunori Takano, Mikako Shirouzu, Kyoko Hanawa-Suetsugu, Takaho Terada, Kiminori Toyooka, Takashi Umehara, Masaki Yamamoto, Shigeyuki Yokoyama, Shiro Suetsugu.
Abstract
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. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID： 20188097 DOI： 10.1016/j.febslet.2010.02.058
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124