Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II

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• 作者：Atsushi Shimada ; Kazunori Takano ; Mikako Shirouzu ; Kyoko Hanawa-Suetsugu ; Takaho Terada ; Kiminori Toyooka ; Takashi Umehara ; Masaki Yamamoto ; Shigeyuki Yokoyama ; Shiro Suetsugu
• 关键词：Membrane ; Protrusion ; Invagination ; EFC domain ; F-BAR domain
• 刊名：FEBS Letters
• 出版年：2010
• 出版时间：19 March 2010
• 年：2010
• 卷：584
• 期：6
• 页码：1111-1118
• 全文大小：2217 K

文摘

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)