Horvath Caroline A J, Vanden Broeck Davy, Boulet Gaëlle A V, Bogers Johannes, De Wolf Marc J S
UA-Laboratory of Cell Biology and Histology, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium.
Int J Biochem Cell Biol. 2007;39(10):1765-70. doi: 10.1016/j.biocel.2006.12.004. Epub 2007 Jan 17.
Epsin was originally discovered by virtue of its binding to another accessory protein, Eps15. Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. Epsin isoforms have been described that differ in intracellular site of action and/or in tissue distribution, although all epsins essentially contribute to membrane deformation. Besides inducing membrane curvature, epsin also plays a key function as adaptor protein, coupling various components of the clathrin-assisted uptake and fulfils an important role in selecting and recognizing cargo. Furthermore, epsin possesses the ability to block vesicle formation during mitosis. To perform all these functions, epsin, apart from interacting with PtdIns(4,5)P2 via its ENTH domain, also engages in several protein interactions with different components of the clathrin-mediated endocytic system. Recently, RNA interference has successfully been exploited to generate a cell line constitutively silencing epsin expression, which can be used to study internalization of multiple ligands.
埃普辛最初是因其与另一种辅助蛋白埃普斯15结合而被发现的。埃普辛家族成员作为辅助蛋白在网格蛋白介导的内吞作用中发挥重要作用。尽管所有埃普辛本质上都有助于膜变形，但已描述的埃普辛同工型在细胞内作用位点和/或组织分布上存在差异。除了诱导膜弯曲外，埃普辛还作为衔接蛋白发挥关键功能，连接网格蛋白辅助摄取的各种成分，并在选择和识别货物中发挥重要作用。此外，埃普辛具有在有丝分裂期间阻断囊泡形成的能力。为了执行所有这些功能，埃普辛除了通过其ENTH结构域与磷脂酰肌醇-4,5-二磷酸（PtdIns(4,5)P2）相互作用外，还与网格蛋白介导的内吞系统的不同成分进行多种蛋白质相互作用。最近，RNA干扰已成功用于生成持续沉默埃普辛表达的细胞系，可用于研究多种配体的内化。
