ENTH/ANTH proteins and clathrin-mediated membrane budding
ENTH/ANTH proteins and clathrin-mediated membrane budding
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DOI：
10.1242/jcs.00928
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发表时间：
2004-01-01
影响因子：
4
通讯作者：
McPherson, PS
中科院分区：
文献类型：
--
作者：
Legendre-Guillemin, V;Wasiak, S;McPherson, PS
epsin n端同源结构域（ENTH）是一个进化上保守的蛋白质模块，主要存在于参与网格蛋白介导的内吞作用的蛋白质中。结构分析和配体结合研究表明，一组先前被指定为携带ENTH结构域的蛋白质实际上包含一个高度相似但独特的模块，称为AP180 n端同源（ANTH）结构域。ENTH和ANTH （E/ANTH）结构域结合肌醇磷脂和蛋白质，并有助于膜上网格蛋白外壳的成核和形成。ENTH结构域还在网格蛋白包被囊泡形成过程中通过脂质重塑参与膜曲率的发展。携带E/ANTH的蛋白最近被证明在反式高尔基网络中与衔接蛋白-1和GGA衔接蛋白一起起作用，这表明E/ANTH结构域是网格蛋白介导的膜出芽机制的普遍组成部分。
The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. Structural analyses and ligand-binding studies have shown that a set of proteins previously designated as harboring an ENTH domain in fact contain a highly similar, yet unique module referred to as an AP180 N-terminal homology (ANTH) domain. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the trans-Golgi network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.