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Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1
SYP51 and 52 are the two members of the SYP5 Qc-SNARE gene family in Arabidopsis thaliana. These two proteins, besides their high level of sequence identity (85%), have shown to have differential functional specificity and possess a different interactome. Here we describe a unique and specific inter...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6334215/ https://www.ncbi.nlm.nih.gov/pubmed/30687352 http://dx.doi.org/10.3389/fpls.2018.01949 |
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author | Barozzi, Fabrizio Papadia, Paride Stefano, Giovanni Renna, Luciana Brandizzi, Federica Migoni, Danilo Fanizzi, Francesco Paolo Piro, Gabriella Di Sansebastiano, Gian-Pietro |
author_facet | Barozzi, Fabrizio Papadia, Paride Stefano, Giovanni Renna, Luciana Brandizzi, Federica Migoni, Danilo Fanizzi, Francesco Paolo Piro, Gabriella Di Sansebastiano, Gian-Pietro |
author_sort | Barozzi, Fabrizio |
collection | PubMed |
description | SYP51 and 52 are the two members of the SYP5 Qc-SNARE gene family in Arabidopsis thaliana. These two proteins, besides their high level of sequence identity (85%), have shown to have differential functional specificity and possess a different interactome. Here we describe a unique and specific interaction of SYP51 with an ER aquaporin, AtNIP1;1 (also known as NLM1) indicated to be able to transport arsenite [As(III)] and previously localized on PM. In the present work we investigate in detail such localization in vivo and characterize the interaction with SYP51. We suggest that this interaction may reveal a new mechanism regulating tonoplast invagination and recycling. We propose this interaction to be part of a regulatory mechanism associated with direct membrane transport from ER to tonoplast and Golgi mediated vesicle trafficking. We also demonstrate that NIP1;1 is important for plant tolerance to arsenite but does not alter its uptake or translocation. To explain such phenomenon the hypothesis that SYP51/NIP1;1 interaction modifies ER and vacuole ability to accumulate arsenite is discussed. |
format | Online Article Text |
id | pubmed-6334215 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-63342152019-01-25 Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 Barozzi, Fabrizio Papadia, Paride Stefano, Giovanni Renna, Luciana Brandizzi, Federica Migoni, Danilo Fanizzi, Francesco Paolo Piro, Gabriella Di Sansebastiano, Gian-Pietro Front Plant Sci Plant Science SYP51 and 52 are the two members of the SYP5 Qc-SNARE gene family in Arabidopsis thaliana. These two proteins, besides their high level of sequence identity (85%), have shown to have differential functional specificity and possess a different interactome. Here we describe a unique and specific interaction of SYP51 with an ER aquaporin, AtNIP1;1 (also known as NLM1) indicated to be able to transport arsenite [As(III)] and previously localized on PM. In the present work we investigate in detail such localization in vivo and characterize the interaction with SYP51. We suggest that this interaction may reveal a new mechanism regulating tonoplast invagination and recycling. We propose this interaction to be part of a regulatory mechanism associated with direct membrane transport from ER to tonoplast and Golgi mediated vesicle trafficking. We also demonstrate that NIP1;1 is important for plant tolerance to arsenite but does not alter its uptake or translocation. To explain such phenomenon the hypothesis that SYP51/NIP1;1 interaction modifies ER and vacuole ability to accumulate arsenite is discussed. Frontiers Media S.A. 2019-01-09 /pmc/articles/PMC6334215/ /pubmed/30687352 http://dx.doi.org/10.3389/fpls.2018.01949 Text en Copyright © 2019 Barozzi, Papadia, Stefano, Renna, Brandizzi, Migoni, Fanizzi, Piro and Di Sansebastiano. 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 Barozzi, Fabrizio Papadia, Paride Stefano, Giovanni Renna, Luciana Brandizzi, Federica Migoni, Danilo Fanizzi, Francesco Paolo Piro, Gabriella Di Sansebastiano, Gian-Pietro Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 |
title | Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 |
title_full | Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 |
title_fullStr | Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 |
title_full_unstemmed | Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 |
title_short | Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1 |
title_sort | variation in membrane trafficking linked to snare atsyp51 interaction with aquaporin nip1;1 |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6334215/ https://www.ncbi.nlm.nih.gov/pubmed/30687352 http://dx.doi.org/10.3389/fpls.2018.01949 |
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