{"language":[{"iso":"eng"}],"_id":"1277","citation":{"mla":"Ortiz Morea, Fausto, et al. “Danger-Associated Peptide Signaling in Arabidopsis Requires Clathrin.” <i>PNAS</i>, vol. 113, no. 39, National Academy of Sciences, 2016, pp. 11028–33, doi:<a href=\"https://doi.org/10.1073/pnas.1605588113\">10.1073/pnas.1605588113</a>.","ieee":"F. Ortiz Morea <i>et al.</i>, “Danger-associated peptide signaling in Arabidopsis requires clathrin,” <i>PNAS</i>, vol. 113, no. 39. National Academy of Sciences, pp. 11028–11033, 2016.","ama":"Ortiz Morea F, Savatin D, Dejonghe W, et al. Danger-associated peptide signaling in Arabidopsis requires clathrin. <i>PNAS</i>. 2016;113(39):11028-11033. doi:<a href=\"https://doi.org/10.1073/pnas.1605588113\">10.1073/pnas.1605588113</a>","ista":"Ortiz Morea F, Savatin D, Dejonghe W, Kumar R, Luo Y, Adamowski M, Van Begin J, Dressano K, De Oliveira G, Zhao X, Lu Q, Madder A, Friml J, De Moura D, Russinova E. 2016. Danger-associated peptide signaling in Arabidopsis requires clathrin. PNAS. 113(39), 11028–11033.","chicago":"Ortiz Morea, Fausto, Daniel Savatin, Wim Dejonghe, Rahul Kumar, Yu Luo, Maciek Adamowski, Jos Van Begin, et al. “Danger-Associated Peptide Signaling in Arabidopsis Requires Clathrin.” <i>PNAS</i>. National Academy of Sciences, 2016. <a href=\"https://doi.org/10.1073/pnas.1605588113\">https://doi.org/10.1073/pnas.1605588113</a>.","apa":"Ortiz Morea, F., Savatin, D., Dejonghe, W., Kumar, R., Luo, Y., Adamowski, M., … Russinova, E. (2016). Danger-associated peptide signaling in Arabidopsis requires clathrin. <i>PNAS</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1605588113\">https://doi.org/10.1073/pnas.1605588113</a>","short":"F. Ortiz Morea, D. Savatin, W. Dejonghe, R. Kumar, Y. Luo, M. Adamowski, J. Van Begin, K. Dressano, G. De Oliveira, X. Zhao, Q. Lu, A. Madder, J. Friml, D. De Moura, E. Russinova, PNAS 113 (2016) 11028–11033."},"doi":"10.1073/pnas.1605588113","page":"11028 - 11033","author":[{"first_name":"Fausto","last_name":"Ortiz Morea","full_name":"Ortiz Morea, Fausto"},{"full_name":"Savatin, Daniel","first_name":"Daniel","last_name":"Savatin"},{"full_name":"Dejonghe, Wim","last_name":"Dejonghe","first_name":"Wim"},{"full_name":"Kumar, Rahul","last_name":"Kumar","first_name":"Rahul"},{"first_name":"Yu","last_name":"Luo","full_name":"Luo, Yu"},{"orcid":"0000-0001-6463-5257","full_name":"Adamowski, Maciek","id":"45F536D2-F248-11E8-B48F-1D18A9856A87","first_name":"Maciek","last_name":"Adamowski"},{"full_name":"Van Begin, Jos","last_name":"Van Begin","first_name":"Jos"},{"last_name":"Dressano","first_name":"Keini","full_name":"Dressano, Keini"},{"full_name":"De Oliveira, Guilherme","last_name":"De Oliveira","first_name":"Guilherme"},{"last_name":"Zhao","first_name":"Xiuyang","full_name":"Zhao, Xiuyang"},{"full_name":"Lu, Qing","last_name":"Lu","first_name":"Qing"},{"full_name":"Madder, Annemieke","first_name":"Annemieke","last_name":"Madder"},{"full_name":"Friml, Jirí","id":"4159519E-F248-11E8-B48F-1D18A9856A87","last_name":"Friml","first_name":"Jirí","orcid":"0000-0002-8302-7596"},{"last_name":"De Moura","first_name":"Daniel","full_name":"De Moura, Daniel"},{"full_name":"Russinova, Eugenia","last_name":"Russinova","first_name":"Eugenia"}],"publication":"PNAS","acknowledgement":"F.A.O.-M. was supported by special\r\nresearch funding from the Flemish Government for a joint doctorate fellowship\r\nat Ghent University, and funding from the Student Program\r\n–\r\nGraduate Studies\r\nPlan Program from the Coordination for the Improvement of Higher Educa-\r\ntion Personnel, Brazil, for a doctorate fellowship at the University of São Paulo.\r\nX.Z. and Q.L. are indebted to the China Science Council and G.P.d.O. to the\r\n“\r\nCiência sem Fronteiras\r\n”\r\nfor predoctoral fellowships. R.K. and Y.L. have re-\r\nceived postdoctoral fellowships from the Belgian Science Policy Office. This\r\nresearch was supported by Flanders Research Foundation Grant G008416N\r\n(to E.R.) and by the São Paulo Research Foundation and the National Council\r\nfor Scientific and Technological Development (CNPq) (D.S.d.M.). D.S.d.M. is a\r\nresearch fellow of CNPq.\r\nWe thank D. Van Damme, E. Mylle, M. Castro Silva-Filho,\r\nand J. Goeman for providing usefu\r\nl advice and technical assistance;\r\nI. Hara-Nishimura, J. Lin, G. Jürgens, M. A. Johnson, and P. Bozhkov for sharing\r\npublished materials; and M. Nowack and M. Fendrych for kindly donating the\r\npUBQ10::ATG8-YFP\r\n-expressing marker line.","year":"2016","volume":113,"publist_id":"6039","intvolume":"       113","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5047203/"}],"abstract":[{"lang":"eng","text":"The Arabidopsis thaliana endogenous elicitor peptides (AtPeps) are released into the apoplast after cellular damage caused by pathogens or wounding to induce innate immunity by direct binding to the membrane-localized leucine-rich repeat receptor kinases, PEP RECEPTOR1 (PEPR1) and PEPR2. Although the PEPR-mediated signaling components and responses have been studied extensively, the contributions of the subcellular localization and dynamics of the active PEPRs remain largely unknown. We used live-cell imaging of the fluorescently labeled and bioactive pep1 to visualize the intracellular behavior of the PEPRs in the Arabidopsis root meristem. We found that AtPep1 decorated the plasma membrane (PM) in a receptor-dependent manner and cointernalized with PEPRs. Trafficking of the AtPep1-PEPR1 complexes to the vacuole required neither the trans-Golgi network/early endosome (TGN/EE)-localized vacuolar H+ -ATPase activity nor the function of the brefeldin A-sensitive ADP-ribosylation factor-guanine exchange factors (ARF-GEFs). In addition, AtPep1 and different TGN/EE markers colocalized only rarely, implying that the intracellular route of this receptor-ligand pair is largely independent of the TGN/EE. Inducible overexpression of the Arabidopsis clathrin coat disassembly factor, Auxilin2, which inhibits clathrin-mediated endocytosis (CME), impaired the AtPep1-PEPR1 internalization and compromised AtPep1-mediated responses. Our results show that clathrin function at the PM is required to induce plant defense responses, likely through CME of cell surface-located signaling components.\r\n"}],"department":[{"_id":"JiFr"}],"issue":"39","publication_status":"published","date_published":"2016-09-27T00:00:00Z","date_updated":"2021-01-12T06:49:34Z","month":"09","day":"27","type":"journal_article","status":"public","title":"Danger-associated peptide signaling in Arabidopsis requires clathrin","quality_controlled":"1","scopus_import":1,"publisher":"National Academy of Sciences","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","date_created":"2018-12-11T11:51:06Z","oa":1,"oa_version":"Preprint"}