RICH-1有一个负责与膜脂结合及脂质体微管形成的BIN/Amphiphysin/Rvsp结构域。
RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes.
作者信息
Richnau Ninna, Fransson Asa, Farsad Khashayar, Aspenström Pontus
机构信息
Ludwig Institute for Cancer Research, Box 595, Biomedical Center, 751 24 Uppsala, Sweden.
出版信息
Biochem Biophys Res Commun. 2004 Jul 30;320(3):1034-42. doi: 10.1016/j.bbrc.2004.05.221.
RhoGAP interacting with CIP4 homologs-1 (RICH-1) was previously found in a yeast two-hybrid screen for proteins interacting with the SH3 domain of the Cdc42-interacting protein 4 (CIP4). RICH-1 was shown to be a RhoGAP for Cdc42 and Rac. In this study, we show that the BIN/Amphiphysin/Rvsp (BAR) domain in RICH-1 confers binding to membrane lipids, and has the potential to deform spherical liposomes into tubes. In accordance with previous findings for the BAR domains in endophilin and amphiphysin, RICH-1-induced tubes appeared striated. We propose that these striated structures are formed by oligomerization of RICH-1 through a putative coiled-coil region within the BAR domain. In support of this notion, we show that RICH-1 forms oligomers in the presence of the chemical cross-linker BS3. These results point to an involvement of RICH-1 in membrane deformation events.
RhoGAP与CIP4同源物-1相互作用蛋白（RICH-1）先前是在酵母双杂交筛选中发现的，该筛选用于寻找与Cdc42相互作用蛋白4（CIP4）的SH3结构域相互作用的蛋白质。研究表明，RICH-1是Cdc42和Rac的RhoGAP。在本研究中，我们发现RICH-1中的BIN/Amphiphysin/Rvsp（BAR）结构域可与膜脂结合，并有可能将球形脂质体变形为管状。与先前关于内吞蛋白和发动蛋白中BAR结构域的研究结果一致，RICH-1诱导形成的管状结构呈现出条纹状。我们推测这些条纹状结构是由RICH-1通过BAR结构域内假定的卷曲螺旋区域寡聚化形成的。为支持这一观点，我们发现RICH-1在化学交联剂BS3存在的情况下会形成寡聚体。这些结果表明RICH-1参与了膜变形事件。
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