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DOI | 10.1073/pnas.2004822117 |
EPSIN1 and MTV1 define functionally overlapping but molecularly distinct trans-Golgi network subdomains in Arabidopsis | |
Heinze L.; Freimuth N.; Rößling A.-K.; Hahnke R.; Riebschläger S.; Fröhlich A.; Sampathkumar A.; McFarlane H.E.; Sauer M. | |
发表日期 | 2020 |
ISSN | 0027-8424 |
起始页码 | 25880 |
结束页码 | 25889 |
卷号 | 117期号:41 |
英文摘要 | The plant trans-Golgi network (TGN) is a central trafficking hub where secretory, vacuolar, recycling, and endocytic pathways merge. Among currently known molecular players involved in TGN transport, three different adaptor protein (AP) complexes promote vesicle generation at the TGN with different cargo specificity and destination. Yet, it remains unresolved how sorting into diverging vesicular routes is spatially organized. Here, we study the family of Arabidopsis thaliana Epsin-like proteins, which are accessory proteins to APs facilitating vesicle biogenesis. By comprehensive molecular, cellular, and genetic analysis of the EPSIN gene family, we identify EPSIN1 and MODIFIED TRANSPORT TO THE VACUOLE1 (MTV1) as its only TGN-associated members. Despite their large phylogenetic distance, they perform overlapping functions in vacuolar and secretory transport. By probing their relationship with AP complexes, we find that they define two molecularly independent pathways:While EPSIN1 associates with AP-1, MTV1 interacts with AP-4, whose function is required for MTV1 recruitment. Although both EPSIN1/AP-1 and MTV1/AP-4 pairs reside at the TGN, high-resolution microscopy reveals them as spatially separate entities. Our results strongly support the hypothesis of molecularly, functionally, and spatially distinct subdomains of the plant TGN and suggest that functional redundancy can be achieved through parallelization of molecularly distinct but functionally overlapping pathways. © 2020 National Academy of Sciences. All rights reserved. |
英文关键词 | Adaptor complexes; ENTH domain; Epsins; Intracellular protein transport; Trans-Golgi network |
语种 | 英语 |
scopus关键词 | adaptor protein; epsin 1; membrane protein; modified transport to the vacuole 1; unclassified drug; Arabidopsis; Article; biogenesis; controlled study; genetic analysis; nonhuman; phylogeny; priority journal; protein protein interaction; protein transport; trans Golgi network |
来源期刊 | Proceedings of the National Academy of Sciences of the United States of America |
文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/160211 |
作者单位 | Heinze, L., Department of Plant Physiology, University of Potsdam, Potsdam, 14476, Germany; Freimuth, N., Department of Plant Physiology, University of Potsdam, Potsdam, 14476, Germany; Rößling, A.-K., Department of Plant Physiology, University of Potsdam, Potsdam, 14476, Germany; Hahnke, R., Department of Plant Physiology, University of Potsdam, Potsdam, 14476, Germany; Riebschläger, S., Department of Plant Physiology, University of Potsdam, Potsdam, 14476, Germany; Fröhlich, A., Max Planck Institute of Molecular Plant Physiology, Potsdam, 14476, Germany; Sampathkumar, A., Max Planck Institute of Molecular Plant Physiology, Potsdam, 14476, Germany; McFarlane, H.E., School of Biosciences, University of Melbourne, Melbourne, VIC 3010, Australia, Department of Cell and Systems Biology, University of Toronto, Toronto, ON M5S 3G5, Canada; Sauer, M., Department of Plant Physiology, University of Potsdam, Potsdam, 14476, Germany |
推荐引用方式 GB/T 7714 | Heinze L.,Freimuth N.,Rößling A.-K.,et al. EPSIN1 and MTV1 define functionally overlapping but molecularly distinct trans-Golgi network subdomains in Arabidopsis[J],2020,117(41). |
APA | Heinze L..,Freimuth N..,Rößling A.-K..,Hahnke R..,Riebschläger S..,...&Sauer M..(2020).EPSIN1 and MTV1 define functionally overlapping but molecularly distinct trans-Golgi network subdomains in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America,117(41). |
MLA | Heinze L.,et al."EPSIN1 and MTV1 define functionally overlapping but molecularly distinct trans-Golgi network subdomains in Arabidopsis".Proceedings of the National Academy of Sciences of the United States of America 117.41(2020). |
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