{"month":"03","date_updated":"2021-01-12T07:40:41Z","type":"journal_article","page":"391 - 397","doi":"10.1016/j.cub.2009.01.057","publication":"Current Biology","day":"10","author":[{"full_name":"Tanaka, Hirokazu","first_name":"Hirokazu","last_name":"Tanaka"},{"first_name":"Saeko","last_name":"Kitakura","full_name":"Kitakura, Saeko"},{"last_name":"De Rycke","first_name":"Riet","full_name":"De Rycke, Riet M"},{"first_name":"Ruth","last_name":"De Groodt","full_name":"De Groodt, Ruth"},{"orcid":"0000-0002-8302-7596","first_name":"Jirí","last_name":"Friml","id":"4159519E-F248-11E8-B48F-1D18A9856A87","full_name":"Jirí Friml"}],"_id":"3048","abstract":[{"text":"Endocytic vesicle trafficking is crucial for regulating activity and localization of plasma membrane components, but the process is still poorly genetically defined in plants. Membrane proteins of the PIN-FORMED (PIN) family exhibit polar localization in plant cells and facilitate cellular efflux of the plant hormone auxin, thereby regulating multiple developmental processes [1, 2]. PIN proteins undergo constitutive endocytosis and GNOM ARF GEF-dependent recycling [3-5], and their localization is under extensive regulation by developmental and environmental cues [6-9]. We designed a fluorescence imaging-based screen to identify Arabidopsis thaliana mutants defective in internalization of proteins including PINs from the plasma membrane. We identified three mutant loci, BFA-visualized endocytic trafficking defective1 (ben1) through ben3 that do not efficiently accumulate PIN1-GFP in intracellular compartments after inhibition of recycling and secretion by fungal toxin brefeldin A (BFA). Fine mapping revealed that BEN1 encodes an ARF GEF vesicle trafficking regulator from the functionally uncharacterized BIG class. ben1 mutant has been previously implicated in pathogen response [10] and shows cell polarity, BFA sensitivity, and growth defects. BEN1 is involved in endocytosis of plasma membrane proteins and localizes to early endocytic compartments distinct from GNOM-positive endosomes. Our results identify BEN1 as the ARF GEF mediating early endosomal traffic.","lang":"eng"}],"extern":1,"date_published":"2009-03-10T00:00:00Z","publication_status":"published","citation":{"ieee":"H. Tanaka, S. Kitakura, R. De Rycke, R. De Groodt, and J. Friml, “Fluorescence imaging based screen identifies ARF GEF component of early endosomal trafficking,” Current Biology, vol. 19, no. 5. Cell Press, pp. 391–397, 2009.","mla":"Tanaka, Hirokazu, et al. “Fluorescence Imaging Based Screen Identifies ARF GEF Component of Early Endosomal Trafficking.” Current Biology, vol. 19, no. 5, Cell Press, 2009, pp. 391–97, doi:10.1016/j.cub.2009.01.057.","short":"H. Tanaka, S. Kitakura, R. De Rycke, R. De Groodt, J. Friml, Current Biology 19 (2009) 391–397.","ama":"Tanaka H, Kitakura S, De Rycke R, De Groodt R, Friml J. Fluorescence imaging based screen identifies ARF GEF component of early endosomal trafficking. Current Biology. 2009;19(5):391-397. doi:10.1016/j.cub.2009.01.057","chicago":"Tanaka, Hirokazu, Saeko Kitakura, Riet De Rycke, Ruth De Groodt, and Jiří Friml. “Fluorescence Imaging Based Screen Identifies ARF GEF Component of Early Endosomal Trafficking.” Current Biology. Cell Press, 2009. https://doi.org/10.1016/j.cub.2009.01.057.","ista":"Tanaka H, Kitakura S, De Rycke R, De Groodt R, Friml J. 2009. Fluorescence imaging based screen identifies ARF GEF component of early endosomal trafficking. Current Biology. 19(5), 391–397.","apa":"Tanaka, H., Kitakura, S., De Rycke, R., De Groodt, R., & Friml, J. (2009). Fluorescence imaging based screen identifies ARF GEF component of early endosomal trafficking. Current Biology. Cell Press. https://doi.org/10.1016/j.cub.2009.01.057"},"issue":"5","publisher":"Cell Press","year":"2009","intvolume":" 19","date_created":"2018-12-11T12:01:03Z","volume":19,"publist_id":"3653","title":"Fluorescence imaging based screen identifies ARF GEF component of early endosomal trafficking","quality_controlled":0,"status":"public"}