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Vacuolar processing enzyme in plant programmed cell death

Vacuolar processing enzyme (VPE) is a cysteine proteinase originally identified as the proteinase responsible for the maturation and activation of vacuolar proteins in plants, and it is known to be an ortholog of animal asparaginyl endopeptidase (AEP/VPE/legumain). VPE has been shown to exhibit enzy...

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Autores principales: Hatsugai, Noriyuki, Yamada, Kenji, Goto-Yamada, Shino, Hara-Nishimura, Ikuko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390986/
https://www.ncbi.nlm.nih.gov/pubmed/25914711
http://dx.doi.org/10.3389/fpls.2015.00234
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author Hatsugai, Noriyuki
Yamada, Kenji
Goto-Yamada, Shino
Hara-Nishimura, Ikuko
author_facet Hatsugai, Noriyuki
Yamada, Kenji
Goto-Yamada, Shino
Hara-Nishimura, Ikuko
author_sort Hatsugai, Noriyuki
collection PubMed
description Vacuolar processing enzyme (VPE) is a cysteine proteinase originally identified as the proteinase responsible for the maturation and activation of vacuolar proteins in plants, and it is known to be an ortholog of animal asparaginyl endopeptidase (AEP/VPE/legumain). VPE has been shown to exhibit enzymatic properties similar to that of caspase 1, which is a cysteine protease that mediates the programmed cell death (PCD) pathway in animals. Although there is limited sequence identity between VPE and caspase 1, their predicted three-dimensional structures revealed that the essential amino-acid residues for these enzymes form similar pockets for the substrate peptide YVAD. In contrast to the cytosolic localization of caspases, VPE is localized in vacuoles. VPE provokes vacuolar rupture, initiating the proteolytic cascade leading to PCD in the plant immune response. It has become apparent that the VPE-dependent PCD pathway is involved not only in the immune response, but also in the responses to a variety of stress inducers and in the development of various tissues. This review summarizes the current knowledge on the contribution of VPE to plant PCD and its role in vacuole-mediated cell death, and it also compares VPE with the animal cell death executor caspase 1.
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spelling pubmed-43909862015-04-24 Vacuolar processing enzyme in plant programmed cell death Hatsugai, Noriyuki Yamada, Kenji Goto-Yamada, Shino Hara-Nishimura, Ikuko Front Plant Sci Plant Science Vacuolar processing enzyme (VPE) is a cysteine proteinase originally identified as the proteinase responsible for the maturation and activation of vacuolar proteins in plants, and it is known to be an ortholog of animal asparaginyl endopeptidase (AEP/VPE/legumain). VPE has been shown to exhibit enzymatic properties similar to that of caspase 1, which is a cysteine protease that mediates the programmed cell death (PCD) pathway in animals. Although there is limited sequence identity between VPE and caspase 1, their predicted three-dimensional structures revealed that the essential amino-acid residues for these enzymes form similar pockets for the substrate peptide YVAD. In contrast to the cytosolic localization of caspases, VPE is localized in vacuoles. VPE provokes vacuolar rupture, initiating the proteolytic cascade leading to PCD in the plant immune response. It has become apparent that the VPE-dependent PCD pathway is involved not only in the immune response, but also in the responses to a variety of stress inducers and in the development of various tissues. This review summarizes the current knowledge on the contribution of VPE to plant PCD and its role in vacuole-mediated cell death, and it also compares VPE with the animal cell death executor caspase 1. Frontiers Media S.A. 2015-04-09 /pmc/articles/PMC4390986/ /pubmed/25914711 http://dx.doi.org/10.3389/fpls.2015.00234 Text en Copyright © 2015 Hatsugai, Yamada, Goto-Yamada and Hara-Nishimura. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Hatsugai, Noriyuki
Yamada, Kenji
Goto-Yamada, Shino
Hara-Nishimura, Ikuko
Vacuolar processing enzyme in plant programmed cell death
title Vacuolar processing enzyme in plant programmed cell death
title_full Vacuolar processing enzyme in plant programmed cell death
title_fullStr Vacuolar processing enzyme in plant programmed cell death
title_full_unstemmed Vacuolar processing enzyme in plant programmed cell death
title_short Vacuolar processing enzyme in plant programmed cell death
title_sort vacuolar processing enzyme in plant programmed cell death
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390986/
https://www.ncbi.nlm.nih.gov/pubmed/25914711
http://dx.doi.org/10.3389/fpls.2015.00234
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AT haranishimuraikuko vacuolarprocessingenzymeinplantprogrammedcelldeath