生物谷訊：本周Science刊登了研究性文章，發(fā)現(xiàn)細(xì)胞膜的形狀感受器,，即細(xì)胞如何感受外力導(dǎo)致細(xì)胞膜彎曲的信號(hào)的分子機(jī)理。這是由英國(guó)科學(xué)家McMahon認(rèn)為是BAR結(jié)構(gòu)域蛋白在其中起關(guān)鍵作用,，BAR（Bin/amphiphysin/Rvs）結(jié)構(gòu)域包括一組蛋白,，amphiphysin與arfaptin2相似是驅(qū)動(dòng)膜的彎曲的主要蛋白，該家族蛋白通過(guò)形成二聚化發(fā)揮作用,，而且該結(jié)構(gòu)域從果蠅到人類都非常保守,，這一研究為細(xì)胞如何感受外界的壓力和容積變化，尤其是神經(jīng)細(xì)胞的突觸傳遞機(jī)理,，內(nèi)皮細(xì)胞的壓力和容積感受（為揭示高血壓和缺血性心臟病提供新的視點(diǎn)）等都具有深遠(yuǎn)的意義,。
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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