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埃普辛1在细胞核与细胞质之间穿梭，其与eps15相互作用的NH(2) -末端同源（ENTH）结构域，在结构上类似于犰狳重复序列和HEAT重复序列，与转录因子早幼粒细胞白血病锌指蛋白（PLZF）相互作用。

Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF).

作者信息

Hyman J, Chen H, Di Fiore P P, De Camilli P, Brunger A T

机构信息

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.

出版信息

J Cell Biol. 2000 May 1;149(3):537-46. doi: 10.1083/jcb.149.3.537.

DOI:10.1083/jcb.149.3.537
PMID:10791968
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2174850/
Abstract

Epsin (Eps15 interactor) is a cytosolic protein involved in clathrin-mediated endocytosis via its direct interactions with clathrin, the clathrin adaptor AP-2, and Eps15. The NH(2)-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH(2)-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 A resolution. This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). Leptomycin B, an antifungal antibiotic, which inhibits the Crm1- dependent nuclear export pathway, induces an accumulation of epsin 1 in the nucleus. These findings suggest that epsin 1 may function in a signaling pathway connecting the endocytic machinery to the regulation of nuclear function.

摘要

Epsin（Eps15相互作用蛋白）是一种胞质蛋白，通过其与网格蛋白、网格蛋白衔接蛋白AP - 2以及Eps15的直接相互作用参与网格蛋白介导的内吞作用。Epsin的NH₂末端部分包含一个功能未知的系统发育保守模块，称为ENTH结构域（Epsin NH₂末端同源结构域）。我们现已解析出大鼠Epsin 1 ENTH结构域的晶体结构，分辨率为1.8 Å。该结构域在结构上分别类似于β-连环蛋白的犰狳重复序列和核转运蛋白β的热重复序列。我们还鉴定并表征了Epsin 1通过ENTH结构域与转录因子早幼粒细胞白血病锌指蛋白（PLZF）的相互作用。抗真菌抗生素 leptomycin B可抑制依赖Crm1的核输出途径，诱导Epsin 1在细胞核中积累。这些发现表明，Epsin 1可能在一条将内吞机制与核功能调节联系起来的信号通路中发挥作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/a2484a385661/JCB0001119.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/f04f50293405/JCB0001119.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/371ed9e6a071/JCB0001119.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/942e15034046/JCB0001119.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/b4d99be1451f/JCB0001119.f4a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/a2484a385661/JCB0001119.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/f04f50293405/JCB0001119.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/371ed9e6a071/JCB0001119.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/942e15034046/JCB0001119.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/b4d99be1451f/JCB0001119.f4a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b01/2174850/a2484a385661/JCB0001119.f5.jpg

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