Ahmed Sohail, Bu Wenyu, Lee Raphael Tze Chuen, Maurer-Stroh Sebastian, Goh Wah Ing
Commun Integr Biol. 2010 Mar;3(2):116-21. doi: 10.4161/cib.3.2.10808.
The F-BAR domain is emerging as an important player in membrane remodeling pathways. F-BAR domain proteins couple membrane remodeling with actin dynamics associated with endocytic pathways and filopodium formation. Here, we provide a comprehensive analysis of F-BAR domain proteins in terms of their evolutionary relationships and protein function. F-BAR domain containing proteins can be categorized into five subfamilies based on their phylogeny which is consistent with the additional protein domains they possess, for example, RhoGAP domains, Cdc42 binding sites, SH3 domains and tyrosine kinase domains. We derive a protein-protein interaction network suggesting that dynamin1/2, N-WASP, Huntingtin, intersectin and Cdc42 are central nodes influencing F-BAR domain protein function.
F-BAR结构域正逐渐成为膜重塑途径中的重要参与者。F-BAR结构域蛋白将膜重塑与内吞途径和丝状伪足形成相关的肌动蛋白动力学联系起来。在这里，我们从进化关系和蛋白质功能方面对F-BAR结构域蛋白进行了全面分析。基于系统发育，含F-BAR结构域的蛋白质可分为五个亚家族，这与它们所拥有的其他蛋白质结构域一致，例如RhoGAP结构域、Cdc42结合位点、SH3结构域和酪氨酸激酶结构域。我们推导了一个蛋白质-蛋白质相互作用网络，表明发动蛋白1/2、N-WASP、亨廷顿蛋白、相交蛋白和Cdc42是影响F-BAR结构域蛋白功能的中心节点。
