I-BAR protein IRSp53 regulates clathrin-independent endocytosis in a biphasic manner
I-BAR protein IRSp53 regulates clathrin-independent endocytosis in a biphasic manner
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I-BAR 蛋白 IRSp53 以双相方式调节网格蛋白独立的内吞作用
DOI：
10.1016/j.scib.2017.12.001
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发表时间：
2018
期刊：
影响因子：
18.9
通讯作者：
Song Eli
中科院分区：
文献类型：
--
作者：
Zhu Xinyu;Xu Xiaojun;Du Kang;Lu Jingze;Song Eli
2017中国科学出版社由Elsevier BV和Science China Press出版。内吞作用是一种基本的细胞活动，在多种生物过程中起着至关重要的作用，包括营养摄取、信号转导、免疫应答、形态发生、神经传递、细胞迁移和组织发育[1-3]。内吞作用分为两种亚型：明确的网格蛋白依赖性内吞作用（CDE）和最近发现的网格蛋白非依赖性内吞作用（CIE）[3]。到目前为止，已经确定了一系列效应器作为CDE过程的调节器。CDE调节剂中最引人注目的一组是BAR（Bin-两性蛋白酶-Rvs）结构域蛋白质超家族，其与肌动蛋白和其他内吞效应物协作以通过协调质膜（PM）中的动态变化来操作内吞囊泡的形成[4]。BAR结构域超家族由三个亚家族组成，包括“经典”BAR、F-BAR（Fes-CIP 4同源BAR）和I-BAR（反向BAR）。BAR亚家族的一个共同特征是BAR的三个反平行螺旋束被单二聚成一个弯曲的模块，该模块具有用于结合膜的带正电的表面。经典的I-BAR结构域和F-BAR结构域呈现凹面并结合正弯曲的膜，而I-BAR结构域呈现凸面并结合负弯曲的膜[4，5]。许多“经典”的BAR结构域蛋白和F-BAR结构域蛋白，如FCHo 2、synd 2、FBP 17、Endo 2、Amph 1和APPL 1，参与CDE过程;一些“经典”的BAR结构域蛋白和F-BAR结构域蛋白，包括endophilin和GRAF 1，参与CIE过程[4，6-9]。然而，I-BAR结构域蛋白MIM在CDE过程中的作用存在争议。加百列Quinones等报道MIM在小鼠胚胎成纤维细胞（MEF）的CDE过程中起负作用[10]，而Meng Cao等发现MIM
© 2017 Science China Press. Published by Elsevier BV and Science China Press. All rights reserved.Endocytosis is a fundamental cellular activity that plays crucial roles in a variety of biological processes, including nutrient uptake, signal transduction, immune response, morphogenesis, neurotransmission, cell migration and tissue development [1–3]. Endocytosis has been classified into two subtypes: the well-defined clathrin-dependent endocytosis (CDE) and the more recently identified clathrin-independent endocytosis (CIE)[3]. So far, a series of effectors have been identified as regulators of the CDE process. One of the most striking groups of CDE regulators is the BAR (Bin-amphipysin-Rvs) domain superfamily of proteins, which collaborates with actin and other endocytic effectors to operate the formation of endocytic vesicles by orchestrating dynamic changes in the plasma membrane (PM)[4]. The BAR domain superfamily is comprised of three subfamilies, including the ‘‘classical” BARs, F-BARs (Fes-CIP4 homology BARs), and I-BARs (Inverse-BARs). A shared feature across the BAR subfamilies is that the three antiparallel helix bundles of the BARs are mono-dimerized into a curved module with a positively charged surface that is used to bind to the membrane.‘‘Classical” BAR domains and F-BAR domains present concave surfaces and bind to positively curved membranes, whereas I-BAR domains present convex surfaces and bind to negatively curved membranes [4, 5]. Many ‘‘classical” BAR domain proteins and F-BAR domain proteins, such as FCHo2, synd2, FBP17, Endo2, Amph1 and APPL1, participate in CDE process; and some ‘‘classical” BAR domain proteins and F-BAR domain proteins, including endophilin and GRAF1, are involved in CIE process [4, 6–9]. However, the role of the I-BAR domain protein MIM in the CDE process is controversial. Gabriel A. Quinones et al. reported that MIM plays a negative role in CDE process in mouse embryonic fibroblast (MEF) cells [10], while Meng Cao et al. found that MIM