Mapping of the basic amino‐acid residues responsible for tubulation and cellular protrusion by the EFC/F‐BAR domain of pacsin2/Syndapin II
Mapping of the basic amino‐acid residues responsible for tubulation and cellular protrusion by the EFC/F‐BAR domain of pacsin2/Syndapin II
复制标题
DOI：
10.1016/j.febslet.2010.02.058
复制
发表时间：
2010-03
期刊：
影响因子：
3.5
通讯作者：
A. Shimada;K. Takano;M. Shirouzu;K. Hanawa-Suetsugu;T. Terada;K. Toyooka;T. Umehara;Masaki Yamamoto;S. Yokoyama;S. Suetsugu
中科院分区：
文献类型：
--
作者：
A. Shimada;K. Takano;M. Shirouzu;K. Hanawa-Suetsugu;T. Terada;K. Toyooka;T. Umehara;Masaki Yamamoto;S. Yokoyama;S. Suetsugu
延伸的Fes-CIP 4同源性（EFC）/FCH-BAR（F-BAR）结构域使膜微管化。pacsin 2 EFC/F-BAR结构域的过表达导致细胞内的管状定位，并在体外使脂质体变形为小管。我们发现pacsin 2 EFC/F-BAR结构域的过表达诱导细胞微刺突，其中pacsin 2 EFC/F-BAR结构域集中在颈部。pacsin 2 EFC/F-BAR结构域凹面上的疏水环和碱性氨基酸残基对于微刺的形成和微管的形成都是必不可少的。由于微钉颈部的曲率和微管的曲率具有相似的几何形状，因此认为pacsin 2 EFC/F-BAR结构域有助于微钉的形成和微管的形成。结构性摘要：MINT-7710892：通过X射线晶体学（MI：0114）测定EFCS pacsin 2（uniprotkb：Q910）和EFCS pacsin 2（uniprotkb：Q910）结合（MI：0407）
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)