钙调蛋白促进N-BAR结构域介导的膜收缩和内吞作用。
Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.
作者信息
Myers Margaret D, Ryazantsev Sergey, Hicke Linda, Payne Gregory S
机构信息
Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Molecular Genetics and Microbiology, College of Natural Sciences, University of Texas at Austin, Austin, TX 78712, USA.
出版信息
Dev Cell. 2016 Apr 18;37(2):162-73. doi: 10.1016/j.devcel.2016.03.012.
Abstract
Membrane remodeling by BAR (Bin, Amphiphysin, RVS) domain-containing proteins, such as endophilins and amphiphysins, is integral to the process of endocytosis. However, little is known about the regulation of endocytic BAR domain activity. We have identified an interaction between the yeast Rvs167 N-BAR domain and calmodulin. Calmodulin-binding mutants of Rvs167 exhibited defects in endocytic vesicle release. In vitro, calmodulin enhanced membrane tubulation and constriction by wild-type Rvs167 but not calmodulin-binding-defective mutants. A subset of mammalian N-BAR domains bound calmodulin, and co-expression of calmodulin with endophilin A2 potentiated tubulation in vivo. These studies reveal a conserved role for calmodulin in regulating the intrinsic membrane-sculpting activity of endocytic N-BAR domains.
摘要
含BAR（Bin、Amphiphysin、RVS）结构域的蛋白（如内吞蛋白和发动蛋白）介导的膜重塑是内吞作用过程所必需的。然而，对于内吞BAR结构域活性的调控却知之甚少。我们发现酵母Rvs167的N-BAR结构域与钙调蛋白之间存在相互作用。Rvs167的钙调蛋白结合突变体在内吞小泡释放方面表现出缺陷。在体外，钙调蛋白可增强野生型Rvs167介导的膜成管和缢缩作用，但对钙调蛋白结合缺陷型突变体则无此作用。一部分哺乳动物N-BAR结构域可结合钙调蛋白，并且在体内，钙调蛋白与内吞蛋白A2共表达可增强成管作用。这些研究揭示了钙调蛋白在调节内吞N-BAR结构域固有膜塑形活性方面的保守作用。
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