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Danger-associated peptide signaling in Arabidopsis requires clathrin

Fausto Andres Ortiz Morea (UGent) , Daniel Savatin (UGent) , Wim Dejonghe (UGent) , Rahul Kumar (UGent) , Yu Luo (UGent) , Maciej Adamowski, Jos Van den Begin (UGent) , Keini Dressano, Guilherme Oliveira (UGent) , Xiuyang Zhao (UGent) , et al.
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Abstract
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-dependentmanner 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.
Keywords
MEMBRANE, COMPLEX, TRAFFICKING, clathrin, endogenous peptides, PEPR, endocytosis, RECEPTOR, THALIANA, DYNAMIC-BEHAVIOR, PLANT DEVELOPMENT, AUXIN TRANSPORTERS, ENDOGENOUS PEPTIDE, MEDIATED ENDOCYTOSIS, Arabidopsis

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Chicago
Ortiz Morea, Fausto Andres, Daniel Savatin, Wim Dejonghe, Rahul Kumar, Yu Luo, Maciej Adamowski, Jos Van den Begin, et al. 2016. “Danger-associated Peptide Signaling in Arabidopsis Requires Clathrin.” Proceedings of the National Academy of Sciences of the United States of America 113 (39): 11028–11033.
APA
Ortiz Morea, F. A., Savatin, D., Dejonghe, W., Kumar, R., Luo, Y., Adamowski, M., Van den Begin, J., et al. (2016). Danger-associated peptide signaling in Arabidopsis requires clathrin. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(39), 11028–11033.
Vancouver
1.
Ortiz Morea FA, Savatin D, Dejonghe W, Kumar R, Luo Y, Adamowski M, et al. Danger-associated peptide signaling in Arabidopsis requires clathrin. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2016;113(39):11028–33.
MLA
Ortiz Morea, Fausto Andres, Daniel Savatin, Wim Dejonghe, et al. “Danger-associated Peptide Signaling in Arabidopsis Requires Clathrin.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 113.39 (2016): 11028–11033. Print.
@article{8174360,
  abstract     = {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-dependentmanner 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.},
  author       = {Ortiz Morea, Fausto Andres and Savatin, Daniel and Dejonghe, Wim and Kumar, Rahul and Luo, Yu and Adamowski, Maciej and Van den Begin, Jos and Dressano, Keini and Oliveira, Guilherme and Zhao, Xiuyang and Lu, Qing and Madder, Annemieke and Friml, Jiri and de Moura, Daniel Scherer and Russinova, Eugenia},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  language     = {eng},
  number       = {39},
  pages        = {11028--11033},
  title        = {Danger-associated peptide signaling in Arabidopsis requires clathrin},
  url          = {http://dx.doi.org/10.1073/pnas.1605588113},
  volume       = {113},
  year         = {2016},
}

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