哺乳动物肌动蛋白结合蛋白1/HIP-55通过调节发动蛋白与肌动蛋白的相互作用，对网格蛋白包被小窝的分裂至关重要。
Mammalian actin-binding protein 1/HIP-55 is essential for the scission of clathrin-coated pits by regulating dynamin-actin interaction.
作者信息
He Kangmin, Xing Rui, Yan Xiaohua, Tian Aiju, Zhang Mingliang, Yuan Jinghe, Lv Zhizhen, Fang Xiaohong, Li Zijian, Zhang Youyi
机构信息
*Institute of Vascular Medicine, Peking University Third Hospital and Academy for Advanced Interdisciplinary Studies, Peking University, Key Laboratory of Cardiovascular Molecular Biology and Regulatory Peptides, Ministry of Health, Key Laboratory of Molecular Cardiovascular Sciences, Ministry of Education and Beijing Key Laboratory of Cardiovascular Receptors Research, Beijing, China; Beijing National Laboratory for Molecular Sciences, Key Laboratory of Molecular Nanostructures and Nanotechnology, Institute of Chemistry, Chinese Academy of Sciences, Beijing, China; and State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.
*Institute of Vascular Medicine, Peking University Third Hospital and Academy for Advanced Interdisciplinary Studies, Peking University, Key Laboratory of Cardiovascular Molecular Biology and Regulatory Peptides, Ministry of Health, Key Laboratory of Molecular Cardiovascular Sciences, Ministry of Education and Beijing Key Laboratory of Cardiovascular Receptors Research, Beijing, China; Beijing National Laboratory for Molecular Sciences, Key Laboratory of Molecular Nanostructures and Nanotechnology, Institute of Chemistry, Chinese Academy of Sciences, Beijing, China; and State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China
出版信息
FASEB J. 2015 Jun;29(6):2495-503. doi: 10.1096/fj.14-264259. Epub 2015 Feb 17.
Actin and dynamin work cooperatively to drive the invagination and scission of clathrin-coated pits (CCPs). However, little is known about the mechanism that orchestrates the spatiotemporal recruitment of dynamin and actin. Here, we have identified the mammalian actin-binding protein 1 (mAbp1; also called HIP-55 or SH3P7), which could bind to clathrin, actin, as well as dynamin, as an adaptor that links the dynamic recruitment of dynamin and actin for the scission of CCPs. Live-cell imaging reveals that mAbp1 is specifically recruited at a late stage of the long-lived CCPs. mAbp1 knockdown impaired CCP scission by reducing dynamin recruitment at the plasma membrane. However, actin disruption remarkably eliminates mAbp1 recruitment and thus dynamin recruitment. These data suggest that by binding to both clathrin and F-actin, mAbp1 is specifically recruited at a late stage of CCP formation, which subsequently recruits dynamin to CCPs.
肌动蛋白和发动蛋白协同作用，驱动网格蛋白包被小窝（CCPs）的内陷和切割。然而，对于协调发动蛋白和肌动蛋白时空募集的机制，人们知之甚少。在这里，我们鉴定出哺乳动物肌动蛋白结合蛋白1（mAbp1；也称为HIP - 55或SH3P7），它可以结合网格蛋白、肌动蛋白以及发动蛋白，作为一种衔接蛋白，将发动蛋白和肌动蛋白的动态募集联系起来，以实现CCPs的切割。活细胞成像显示，mAbp1在长寿CCPs的后期被特异性募集。mAbp1基因敲低通过减少质膜上发动蛋白的募集而损害CCP切割。然而，肌动蛋白的破坏显著消除了mAbp1的募集，从而也消除了发动蛋白的募集。这些数据表明，通过结合网格蛋白和F - 肌动蛋白，mAbp1在CCP形成的后期被特异性募集，随后将发动蛋白募集到CCPs上。
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