生物谷讯：本周Science刊登了研究性文章，发现细胞膜的形状感受器，即细胞如何感受外力导致细胞膜弯曲的信号的分子机理。这是由英国科学家McMahon认为是BAR结构域蛋白在其中起关键作用，BAR（Bin/amphiphysin/Rvs）结构域包括一组蛋白，amphiphysin与arfaptin2相似是驱动膜的弯曲的主要蛋白，该家族蛋白通过形成二聚化发挥作用，而且该结构域从果蝇到人类都非常保守，这一研究为细胞如何感受外界的压力和容积变化，尤其是神经细胞的突触传递机理，内皮细胞的压力和容积感受（为揭示高血压和缺血性心脏病提供新的视点）等都具有深远的意义。
BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
Brian J. Peter,* Helen M. Kent,* Ian G. Mills, Yvonne Vallis, P. Jonathan G. Butler, Philip R. Evans, Harvey T. McMahon
Science, Vol. 303, Issue 5657, 495-499, January 23, 2004
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
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