酵母 epsins 含有一个必需的 N 端 ENTH 结构域，能结合网格蛋白，是内吞作用所必需的。
Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis.
作者信息
Wendland B, Steece K E, Emr S D
机构信息
Department of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA.
出版信息
EMBO J. 1999 Aug 16;18(16):4383-93. doi: 10.1093/emboj/18.16.4383.
The mammalian protein epsin is required for endocytosis. In this study, we have characterized two homologous yeast proteins, Ent1p and Ent2p, which are similar to mammalian epsin. An essential function for the highly conserved N-terminal epsin N-terminal homology (ENTH) domain was revealed using deletions and randomly generated temperature-sensitive ent1 alleles. Changes in conserved ENTH domain residues in ent1(ts) cells revealed defects in endocytosis and actin cytoskeleton structure. The Ent1 protein was localized to peripheral and internal punctate structures, and biochemical fractionation studies found the protein associated with a large, Triton X-100-insoluble pellet. Finally, an Ent1p clathrin-binding domain was mapped to the final eight amino acids (RGYTLIDL*) in the Ent1 protein sequence. Based on these and other data, we propose that the yeast epsin-like proteins are essential components of an endocytic complex that may act at multiple stages in the endocytic pathway.
哺乳动物蛋白 epsin 是内吞作用所必需的。在本研究中，我们鉴定了两种与哺乳动物 epsin 相似的同源酵母蛋白 Ent1p 和 Ent2p。利用缺失和随机产生的温度敏感型 ent1 等位基因揭示了高度保守的 N 端 epsin N 端同源性（ENTH）结构域的重要功能。ent1(ts) 细胞中保守的 ENTH 结构域残基的变化揭示了内吞作用和肌动蛋白细胞骨架结构的缺陷。Ent1 蛋白定位于外周和内部点状结构，生化分级分离研究发现该蛋白与一个大的、不溶于 Triton X-100 的沉淀相关。最后，Ent1p 网格蛋白结合结构域被定位到 Ent1 蛋白序列的最后八个氨基酸（RGYTLIDL*）。基于这些及其他数据，我们提出酵母类 epsin 蛋白是内吞复合物的重要组成部分，可能在内吞途径中的多个阶段发挥作用。
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