定位 pacsin2/Syndapin II 的 EFC/F-BAR 结构域导致管腔形成和细胞突出的基本氨基酸残基。

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

机构信息

RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama, Japan.

出版信息

FEBS Lett. 2010 Mar 19;584(6):1111-8. doi: 10.1016/j.febslet.2010.02.058. Epub 2010 Feb 24.

DOI:10.1016/j.febslet.2010.02.058

PMID:20188097

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.

摘要

延伸的 Fes-CIP4 同源结构域（EFC）/FCH-BAR（F-BAR）结构域可使膜形成管状结构。pacsin2 的 EFC/F-BAR 结构域过表达会导致细胞内的管状结构定位，并使体外的脂质体变形为管状。我们发现 pacsin2 的 EFC/F-BAR 结构域过表达会诱导细胞微刺的形成，其中 pacsin2 的 EFC/F-BAR 结构域集中在颈部。pacsin2 的 EFC/F-BAR 结构域凹面的疏水性环和碱性氨基酸残基对于微刺的形成和管状化都是必需的。由于微刺颈部的曲率和管状化的曲率具有相似的几何形状，因此 pacsin2 的 EFC/F-BAR 结构域被认为可以促进微刺的形成和管状化。