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

Atsushi Shimada, Kazunori Takano, Mikako Shirouzu, Kyoko Hanawa-Suetsugu, Takaho Terada, Kiminori Toyooka, Takashi Umehara, Masaki Yamamoto, Shigeyuki Yokoyama, Shiro Suetsugu

研究成果: ジャーナルへの寄稿記事

50 引用 (Scopus)

抜粋

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.

元の言語英語
ページ(範囲)1111-1118
ページ数8
ジャーナルFEBS Letters
584
発行部数6
DOI
出版物ステータス出版済み - 3 1 2010
外部発表Yes

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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