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学科主题临床医学
Mammalian actin-binding protein 1/HIP-55 is essential for the scission of clathrin-coated pits by regulating dynamin-actin interaction
He, Kangmin1,2,3,4; Xing, Rui1,2,3; Yan, Xiaohua5; Tian, Aiju1,2,3; Zhang, Mingliang1,2,3; Yuan, Jinghe4; Lv, Zhizhen1,2,3; Fang, Xiaohong4; Li, Zijian1,2,3; Zhang, Youyi1,2,3
关键词Membrane Trafficking Adaptor Protein Quantitative Live-cell Imaging
刊名FASEB JOURNAL
2015-06-01
DOI10.1096/fj.14-264259
29期:6页:2495-2503
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Biology ; Cell Biology
研究领域[WOS]Biochemistry & Molecular Biology ; Life Sciences & Biomedicine - Other Topics ; Cell Biology
关键词[WOS]MEDIATED ENDOCYTOSIS ; ADAPTER PROTEIN ; CYTOSKELETON ; ACTIVATION ; RECEPTORS ; GTPASE
英文摘要

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 toclathrin, 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.

语种英语
WOS记录号WOS:000355209500026
项目编号2013CB933701 ; 2012CB518000 ; 2011CB503903 ; 81471893 ; 81070078 ; 81270157 ; 81270159
资助机构National Key Basic Research Program of the People&prime ; s Republic of China ; Natural Science Foundation of China ; Emory Global Health Institute (Atlanta, GA, USA)
引用统计
被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/58086
专题北京大学第三临床医学院_心血管内科
作者单位1.Peking Univ, Hosp 3, Inst Vasc Med, Beijing 100871, Peoples R China
2.Peking Univ, Acad Adv Interdisciplinary Studies, Key Lab Cardiovascular Mol Biol & Regulatory Pept, Key Lab Mol Cardiovasc Sci,Minist Educ,Minist Hlt, Beijing 100871, Peoples R China
3.Beijing Key Lab Cardiovasc Receptors Res, Beijing 100871, Peoples R China
4.Chinese Acad Sci, Inst Chem, Key Lab Mol Nanostruct & Nanotechnol, Beijing Natl Lab Mol Sci, Beijing 100080, Peoples R China
5.Tsinghua Univ, Tsinghua Peking Ctr Life Sci, Sch Life Sci, Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
推荐引用方式
GB/T 7714
He, Kangmin,Xing, Rui,Yan, Xiaohua,et al. Mammalian actin-binding protein 1/HIP-55 is essential for the scission of clathrin-coated pits by regulating dynamin-actin interaction[J]. FASEB JOURNAL,2015,29(6):2495-2503.
APA He, Kangmin.,Xing, Rui.,Yan, Xiaohua.,Tian, Aiju.,Zhang, Mingliang.,...&Zhang, Youyi.(2015).Mammalian actin-binding protein 1/HIP-55 is essential for the scission of clathrin-coated pits by regulating dynamin-actin interaction.FASEB JOURNAL,29(6),2495-2503.
MLA He, Kangmin,et al."Mammalian actin-binding protein 1/HIP-55 is essential for the scission of clathrin-coated pits by regulating dynamin-actin interaction".FASEB JOURNAL 29.6(2015):2495-2503.
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