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Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain

Lipid droplets (LDs) are neutral-lipid-containing organelles found in all kingdoms of life and are coated with proteins that carry out a vast array of functions. Compared to mammals and yeast, relatively few LD proteins have been identified in plants, particularly those associated with LDs in vegeta...

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Autores principales: Doner, Nathan M., Seay, Damien, Mehling, Marina, Sun, Siqi, Gidda, Satinder K., Schmitt, Kerstin, Braus, Gerhard H., Ischebeck, Till, Chapman, Kent D., Dyer, John M., Mullen, Robert T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8079945/
https://www.ncbi.nlm.nih.gov/pubmed/33936146
http://dx.doi.org/10.3389/fpls.2021.658961
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author Doner, Nathan M.
Seay, Damien
Mehling, Marina
Sun, Siqi
Gidda, Satinder K.
Schmitt, Kerstin
Braus, Gerhard H.
Ischebeck, Till
Chapman, Kent D.
Dyer, John M.
Mullen, Robert T.
author_facet Doner, Nathan M.
Seay, Damien
Mehling, Marina
Sun, Siqi
Gidda, Satinder K.
Schmitt, Kerstin
Braus, Gerhard H.
Ischebeck, Till
Chapman, Kent D.
Dyer, John M.
Mullen, Robert T.
author_sort Doner, Nathan M.
collection PubMed
description Lipid droplets (LDs) are neutral-lipid-containing organelles found in all kingdoms of life and are coated with proteins that carry out a vast array of functions. Compared to mammals and yeast, relatively few LD proteins have been identified in plants, particularly those associated with LDs in vegetative (non-seed) cell types. Thus, to better understand the cellular roles of LDs in plants, a more comprehensive inventory and characterization of LD proteins is required. Here, we performed a proteomics analysis of LDs isolated from drought-stressed Arabidopsis leaves and identified EARLY RESPONSIVE TO DEHYDRATION 7 (ERD7) as a putative LD protein. mCherry-tagged ERD7 localized to both LDs and the cytosol when ectopically expressed in plant cells, and the protein’s C-terminal senescence domain (SD) was both necessary and sufficient for LD targeting. Phylogenetic analysis revealed that ERD7 belongs to a six-member family in Arabidopsis that, along with homologs in other plant species, is separated into two distinct subfamilies. Notably, the SDs of proteins from each subfamily conferred targeting to either LDs or mitochondria. Further, the SD from the ERD7 homolog in humans, spartin, localized to LDs in plant cells, similar to its localization in mammals; although, in mammalian cells, spartin also conditionally localizes to other subcellular compartments, including mitochondria. Disruption of ERD7 gene expression in Arabidopsis revealed no obvious changes in LD numbers or morphology under normal growth conditions, although this does not preclude a role for ERD7 in stress-induced LD dynamics. Consistent with this possibility, a yeast two-hybrid screen using ERD7 as bait identified numerous proteins involved in stress responses, including some that have been identified in other LD proteomes. Collectively, these observations provide new insight to ERD7 and the SD-containing family of proteins in plants and suggest that ERD7 may be involved in functional aspects of plant stress response that also include localization to the LD surface.
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spelling pubmed-80799452021-04-29 Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain Doner, Nathan M. Seay, Damien Mehling, Marina Sun, Siqi Gidda, Satinder K. Schmitt, Kerstin Braus, Gerhard H. Ischebeck, Till Chapman, Kent D. Dyer, John M. Mullen, Robert T. Front Plant Sci Plant Science Lipid droplets (LDs) are neutral-lipid-containing organelles found in all kingdoms of life and are coated with proteins that carry out a vast array of functions. Compared to mammals and yeast, relatively few LD proteins have been identified in plants, particularly those associated with LDs in vegetative (non-seed) cell types. Thus, to better understand the cellular roles of LDs in plants, a more comprehensive inventory and characterization of LD proteins is required. Here, we performed a proteomics analysis of LDs isolated from drought-stressed Arabidopsis leaves and identified EARLY RESPONSIVE TO DEHYDRATION 7 (ERD7) as a putative LD protein. mCherry-tagged ERD7 localized to both LDs and the cytosol when ectopically expressed in plant cells, and the protein’s C-terminal senescence domain (SD) was both necessary and sufficient for LD targeting. Phylogenetic analysis revealed that ERD7 belongs to a six-member family in Arabidopsis that, along with homologs in other plant species, is separated into two distinct subfamilies. Notably, the SDs of proteins from each subfamily conferred targeting to either LDs or mitochondria. Further, the SD from the ERD7 homolog in humans, spartin, localized to LDs in plant cells, similar to its localization in mammals; although, in mammalian cells, spartin also conditionally localizes to other subcellular compartments, including mitochondria. Disruption of ERD7 gene expression in Arabidopsis revealed no obvious changes in LD numbers or morphology under normal growth conditions, although this does not preclude a role for ERD7 in stress-induced LD dynamics. Consistent with this possibility, a yeast two-hybrid screen using ERD7 as bait identified numerous proteins involved in stress responses, including some that have been identified in other LD proteomes. Collectively, these observations provide new insight to ERD7 and the SD-containing family of proteins in plants and suggest that ERD7 may be involved in functional aspects of plant stress response that also include localization to the LD surface. Frontiers Media S.A. 2021-04-14 /pmc/articles/PMC8079945/ /pubmed/33936146 http://dx.doi.org/10.3389/fpls.2021.658961 Text en Copyright © 2021 Doner, Seay, Mehling, Sun, Gidda, Schmitt, Braus, Ischebeck, Chapman, Dyer and Mullen. https://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
Doner, Nathan M.
Seay, Damien
Mehling, Marina
Sun, Siqi
Gidda, Satinder K.
Schmitt, Kerstin
Braus, Gerhard H.
Ischebeck, Till
Chapman, Kent D.
Dyer, John M.
Mullen, Robert T.
Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain
title Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain
title_full Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain
title_fullStr Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain
title_full_unstemmed Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain
title_short Arabidopsis thaliana EARLY RESPONSIVE TO DEHYDRATION 7 Localizes to Lipid Droplets via Its Senescence Domain
title_sort arabidopsis thaliana early responsive to dehydration 7 localizes to lipid droplets via its senescence domain
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8079945/
https://www.ncbi.nlm.nih.gov/pubmed/33936146
http://dx.doi.org/10.3389/fpls.2021.658961
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