Letter to the Editor:: NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana
Letter to the Editor:: NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana
复制标题
DOI：
10.1023/b:jnmr.0000019239.44783.66
复制
发表时间：
2004-06-01
影响因子：
2.7
通讯作者：
Güntert, P
中科院分区：
文献类型：
--
作者：
López-Méndez, B;Pantoja-Uceda, D;Güntert, P
网格蛋白介导的内吞作用涉及多种胞质蛋白，它们相互配合以选择内吞小泡的内容物，并诱导新形成的内吞小泡内陷、分裂和释放到胞质中。胞质内吞机制中最具特征的成分是外壳蛋白网格蛋白和接头复合物 AP2。两者都是包被囊泡的结构成分。此外，其他几种蛋白质（称为“辅助”蛋白质）被认为在内吞作用中起主要调节作用（Wendland，2002）。 ENTH（epsin N 端同源性；Chen 等，1998）和 VHS（Vps27、Hrs 和 STAM；Schultz 等，1998）结构域存在于许多“辅助”蛋白的 N 端部分。它们与膜磷脂相互作用的实验证据表明，这两个结构域在网格蛋白包被的囊泡形成的第一步中都发挥着作用。来自拟南芥的假设 ENTH-VHS 结构域 At3g16270 是一种 127 个氨基酸的蛋白质，被 RIKEN 结构基因组学/蛋白质组学计划选择用于 NMR 研究 （RSGI）（横山等人，2000）。通过远距离氨基酸序列相似性预测该假设蛋白质中存在 ENTH 或 VHS 结构域。
Clathrin-mediated endocytosis involves several cytosolic proteins that cooperate with each other to select the content of the endocytic vesicles, and to induce the invagination, scission and release of the newly formed endocytic vesicle into the cytosol. The bestcharacterized components of the cytosolic endocytic machinery are the coat protein clathrin and the adaptor complex AP2. Both are structural components of the coated vesicles. In addition, several other proteins, known as ‘accessory’proteins are considered to have primarily regulatory roles in the endocytosis (Wendland, 2002). ENTH (epsin N-terminal homology; Chen et al., 1998) and VHS (Vps27, Hrs and STAM; Schultz et al., 1998) domains are present in the N-terminal part of many ‘accessory’proteins. Experimental evidence of their interaction with membrane phospholipids suggests for both domains a role in the first steps of the formation of the clathrin-coated vesicles.The hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana is a 127 amino acid protein that was selected for NMR study by the RIKEN Structural Genomics/Proteomics Initiative (RSGI)(Yokoyama et al., 2000). The presence of an ENTH or a VHS domain in this hypothetical protein is predicted by distant amino acid sequence similarity.