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Danger-associated peptide signaling in Arabidopsis requires clathrin

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 th... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America 27 September 2016, Vol.113(39), pp.11028-33
Main Author: Ortiz-Morea, Fausto Andres
Other Authors: Savatin, Daniel V , Dejonghe, Wim , Kumar, Rahul , Luo, Yu , Adamowski, Maciej , Van Den Begin, Jos , Dressano, Keini , Pereira De Oliveira, Guilherme , Zhao, Xiuyang , Lu, Qing , Madder, Annemieke , Friml, Jiří , Scherer De Moura, Daniel , Russinova, Eugenia
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; PMID: 27651494 Version:1 ; DOI: 10.1073/pnas.1605588113
Link: http://pubmed.gov/27651494
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title: Danger-associated peptide signaling in Arabidopsis requires clathrin
format: Article
creator:
  • Ortiz-Morea, Fausto Andres
  • Savatin, Daniel V
  • Dejonghe, Wim
  • Kumar, Rahul
  • Luo, Yu
  • Adamowski, Maciej
  • Van Den Begin, Jos
  • Dressano, Keini
  • Pereira De Oliveira, Guilherme
  • Zhao, Xiuyang
  • Lu, Qing
  • Madder, Annemieke
  • Friml, Jiří
  • Scherer De Moura, Daniel
  • Russinova, Eugenia
subjects:
  • Arabidopsis
  • Pepr
  • Clathrin
  • Endocytosis
  • Endogenous Peptides
  • Signal Transduction
  • Arabidopsis -- Metabolism
  • Clathrin -- Metabolism
  • Peptides -- Metabolism
ispartof: Proceedings of the National Academy of Sciences of the United States of America, 27 September 2016, Vol.113(39), pp.11028-33
description: 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.
language: eng
source:
identifier: E-ISSN: 1091-6490 ; PMID: 27651494 Version:1 ; DOI: 10.1073/pnas.1605588113
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleDanger-associated peptide signaling in Arabidopsis requires clathrin
creatorOrtiz-Morea, Fausto Andres ; Savatin, Daniel V ; Dejonghe, Wim ; Kumar, Rahul ; Luo, Yu ; Adamowski, Maciej ; Van Den Begin, Jos ; Dressano, Keini ; Pereira De Oliveira, Guilherme ; Zhao, Xiuyang ; Lu, Qing ; Madder, Annemieke ; Friml, Jiří ; Scherer De Moura, Daniel ; Russinova, Eugenia
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subjectArabidopsis ; Pepr ; Clathrin ; Endocytosis ; Endogenous Peptides ; Signal Transduction ; Arabidopsis -- Metabolism ; Clathrin -- Metabolism ; Peptides -- Metabolism
descriptionThe 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.
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titleDanger-associated peptide signaling in Arabidopsis requires clathrin
descriptionThe 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.
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authorOrtiz-Morea, Fausto Andres ; Savatin, Daniel V ; Dejonghe, Wim ; Kumar, Rahul ; Luo, Yu ; Adamowski, Maciej ; Van Den Begin, Jos ; Dressano, Keini ; Pereira De Oliveira, Guilherme ; Zhao, Xiuyang ; Lu, Qing ; Madder, Annemieke ; Friml, Jiří ; Scherer De Moura, Daniel ; Russinova, Eugenia
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abstractThe 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.
doi10.1073/pnas.1605588113
pmid27651494
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date2016-09-27