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The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto

The tomato (Solanum lycopersicum) AGC protein kinase Adi3 functions as a suppressor of cell death and was first identified as an interactor with the tomato resistance protein Pto and the Pseudomonas syringae effector protein AvrPto. Models predict that loss of Adi3 cell death suppression (CDS) activ...

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Autores principales: Ek-Ramos, María J., Avila, Julian, Nelson Dittrich, Anna C., Su, Dongyin, Gray, Joel W., Devarenne, Timothy P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4211712/
https://www.ncbi.nlm.nih.gov/pubmed/25350368
http://dx.doi.org/10.1371/journal.pone.0110807
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author Ek-Ramos, María J.
Avila, Julian
Nelson Dittrich, Anna C.
Su, Dongyin
Gray, Joel W.
Devarenne, Timothy P.
author_facet Ek-Ramos, María J.
Avila, Julian
Nelson Dittrich, Anna C.
Su, Dongyin
Gray, Joel W.
Devarenne, Timothy P.
author_sort Ek-Ramos, María J.
collection PubMed
description The tomato (Solanum lycopersicum) AGC protein kinase Adi3 functions as a suppressor of cell death and was first identified as an interactor with the tomato resistance protein Pto and the Pseudomonas syringae effector protein AvrPto. Models predict that loss of Adi3 cell death suppression (CDS) activity during Pto/AvrPto interaction leads to the cell death associated with the resistance response initiated from this interaction. Nuclear localization is required for Adi3 CDS. Prevention of nuclear accumulation eliminates Adi3 CDS and induces cell death by localizing Adi3 to intracellular punctate membrane structures. Here we use several markers of the endomembrane system to show that the punctate membrane structures to which non-nuclear Adi3 is localized are endosomal in nature. Wild-type Adi3 also localizes in these punctate endosomal structures. This was confirmed by the use of endosomal trafficking inhibitors, which were capable of trapping wild-type Adi3 in endosomal-like structures similar to the non-nuclear Adi3. This suggests Adi3 may traffic through the cell using the endomembrane system. Additionally, Adi3 was no longer found in the nucleus but was visualized in these punctate endosomal-like membranes during the cell death induced by the Pto/AvrPto interaction. Therefore we propose that inhibiting nuclear import and constraining Adi3 to the endosomal system in response to AvrPto is a mechanism to initiate the cell death associated with resistance.
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spelling pubmed-42117122014-11-05 The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto Ek-Ramos, María J. Avila, Julian Nelson Dittrich, Anna C. Su, Dongyin Gray, Joel W. Devarenne, Timothy P. PLoS One Research Article The tomato (Solanum lycopersicum) AGC protein kinase Adi3 functions as a suppressor of cell death and was first identified as an interactor with the tomato resistance protein Pto and the Pseudomonas syringae effector protein AvrPto. Models predict that loss of Adi3 cell death suppression (CDS) activity during Pto/AvrPto interaction leads to the cell death associated with the resistance response initiated from this interaction. Nuclear localization is required for Adi3 CDS. Prevention of nuclear accumulation eliminates Adi3 CDS and induces cell death by localizing Adi3 to intracellular punctate membrane structures. Here we use several markers of the endomembrane system to show that the punctate membrane structures to which non-nuclear Adi3 is localized are endosomal in nature. Wild-type Adi3 also localizes in these punctate endosomal structures. This was confirmed by the use of endosomal trafficking inhibitors, which were capable of trapping wild-type Adi3 in endosomal-like structures similar to the non-nuclear Adi3. This suggests Adi3 may traffic through the cell using the endomembrane system. Additionally, Adi3 was no longer found in the nucleus but was visualized in these punctate endosomal-like membranes during the cell death induced by the Pto/AvrPto interaction. Therefore we propose that inhibiting nuclear import and constraining Adi3 to the endosomal system in response to AvrPto is a mechanism to initiate the cell death associated with resistance. Public Library of Science 2014-10-28 /pmc/articles/PMC4211712/ /pubmed/25350368 http://dx.doi.org/10.1371/journal.pone.0110807 Text en © 2014 Ek-Ramos et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ek-Ramos, María J.
Avila, Julian
Nelson Dittrich, Anna C.
Su, Dongyin
Gray, Joel W.
Devarenne, Timothy P.
The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto
title The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto
title_full The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto
title_fullStr The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto
title_full_unstemmed The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto
title_short The Tomato Cell Death Suppressor Adi3 Is Restricted to the Endosomal System in Response to the Pseudomonas syringae Effector Protein AvrPto
title_sort tomato cell death suppressor adi3 is restricted to the endosomal system in response to the pseudomonas syringae effector protein avrpto
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4211712/
https://www.ncbi.nlm.nih.gov/pubmed/25350368
http://dx.doi.org/10.1371/journal.pone.0110807
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