p115拴系蛋白中一个隐秘的Rab1结合位点。
A cryptic Rab1-binding site in the p115 tethering protein.
作者信息
Beard Matthew, Satoh Ayano, Shorter James, Warren Graham
机构信息
Department of Physiology and Cellular Biophysics, Columbia University, New York, New York 10032, USA.
出版信息
J Biol Chem. 2005 Jul 8;280(27):25840-8. doi: 10.1074/jbc.M503925200. Epub 2005 May 6.
Small GTPases and coiled-coil proteins of the golgin family help to tether COPI vesicles to Golgi membranes. At the cis-side of the Golgi, the Rab1 GTPase binds directly to each of three coiled-coil proteins: p115, GM130, and as now shown, Giantin. Rab1 binds to a coiled-coil region within the tail domain of p115 and this binding is inhibited by the C-terminal, acidic domain of p115. Furthermore, GM130 and Giantin bind to the acidic domain of p115 and stimulate p115 binding to Rab1, suggesting that p115 binding to Rab1 is regulated. Regulation of this interaction by proteins such as GM130 and Giantin may control the membrane recruitment of p115 by Rab1.
小GTP酶和高尔基体蛋白家族的卷曲螺旋蛋白有助于将COPI囊泡拴系到高尔基体膜上。在高尔基体的顺面，Rab1 GTP酶直接结合三种卷曲螺旋蛋白中的每一种：p115、GM130，以及现在发现的巨蛋白（Giantin）。Rab1结合到p115尾部结构域内的一个卷曲螺旋区域，并且这种结合被p115的C末端酸性结构域所抑制。此外，GM130和巨蛋白结合到p115的酸性结构域并刺激p115与Rab1的结合，这表明p115与Rab1的结合是受调控的。GM130和巨蛋白等蛋白质对这种相互作用的调控可能控制Rab1对p115的膜招募。
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