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Plant Vacuolar Processing Enzymes

Plant proteomes contain hundreds of proteases divided into different families based on evolutionary and functional relationship. In particular, plant cysteine proteases of the C1 (papain-like) and C13 (legumain-like) families play key roles in many physiological processes. The legumain-like protease...

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Autores principales: Vorster, Barend Juan, Cullis, Christopher A., Kunert, Karl J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6473326/
https://www.ncbi.nlm.nih.gov/pubmed/31031794
http://dx.doi.org/10.3389/fpls.2019.00479
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author Vorster, Barend Juan
Cullis, Christopher A.
Kunert, Karl J.
author_facet Vorster, Barend Juan
Cullis, Christopher A.
Kunert, Karl J.
author_sort Vorster, Barend Juan
collection PubMed
description Plant proteomes contain hundreds of proteases divided into different families based on evolutionary and functional relationship. In particular, plant cysteine proteases of the C1 (papain-like) and C13 (legumain-like) families play key roles in many physiological processes. The legumain-like proteases, also called vacuolar processing enzymes (VPEs), perform a multifunctional role in different plant organs and during different stages of plant development and death. VPEs are similar to animal caspases, and although caspase activity was identified in plants almost 40 years ago, there still remains much research to be done to gain a complete understanding of their various roles and functions in plants. Here we not only summarize the current existing knowledge of plant VPEs, including recent developments in the field, but also highlight the future prospective areas to be investigated to obtain a more detailed understanding of the role of VPEs in plants.
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spelling pubmed-64733262019-04-26 Plant Vacuolar Processing Enzymes Vorster, Barend Juan Cullis, Christopher A. Kunert, Karl J. Front Plant Sci Plant Science Plant proteomes contain hundreds of proteases divided into different families based on evolutionary and functional relationship. In particular, plant cysteine proteases of the C1 (papain-like) and C13 (legumain-like) families play key roles in many physiological processes. The legumain-like proteases, also called vacuolar processing enzymes (VPEs), perform a multifunctional role in different plant organs and during different stages of plant development and death. VPEs are similar to animal caspases, and although caspase activity was identified in plants almost 40 years ago, there still remains much research to be done to gain a complete understanding of their various roles and functions in plants. Here we not only summarize the current existing knowledge of plant VPEs, including recent developments in the field, but also highlight the future prospective areas to be investigated to obtain a more detailed understanding of the role of VPEs in plants. Frontiers Media S.A. 2019-04-12 /pmc/articles/PMC6473326/ /pubmed/31031794 http://dx.doi.org/10.3389/fpls.2019.00479 Text en Copyright © 2019 Vorster, Cullis and Kunert. 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) and the copyright owner(s) 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
Vorster, Barend Juan
Cullis, Christopher A.
Kunert, Karl J.
Plant Vacuolar Processing Enzymes
title Plant Vacuolar Processing Enzymes
title_full Plant Vacuolar Processing Enzymes
title_fullStr Plant Vacuolar Processing Enzymes
title_full_unstemmed Plant Vacuolar Processing Enzymes
title_short Plant Vacuolar Processing Enzymes
title_sort plant vacuolar processing enzymes
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6473326/
https://www.ncbi.nlm.nih.gov/pubmed/31031794
http://dx.doi.org/10.3389/fpls.2019.00479
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