Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv]
In Arabidopsis the borate transporter BOR1, which is located in the plasma membrane, is degraded in the presence of excess boron by an endocytosis-mediated mechanism. A similar mechanism was suggested in rice as excess boron decreased rice borate transporter levels, although in this case whether the...
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doaj-523838e93025441dbc5dd3c6f379c49b2020-11-25T03:14:21ZengF1000 Research LtdF1000Research2046-14022013-09-01210.12688/f1000research.2-185.v1751Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv]Noboru Yamauchi0Tadashi Gosho1Satoru Asatuma2Kiminori Toyooka3Toru Fujiwara4Ken Matsuoka5Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, 812-8581, JapanBiotechnology Research Center, The University of Tokyo, Tokyo, 113-8657, JapanCurrent address: Omu Milk Products Co., Ltd., Omuta, 836-0895, JapanCurrent address: RIKEN Center for Sustainable Resource Science, Yokohama, 230-0045, JapanCurrent address: Laboratory of Plant Nutrition and Fertilizer, Graduate School of Agricultural and Life Science, The University of Tokyo, Tokyo, 113-8657, JapanBiotron Application Center, Kyushu University, Fukuoka, 812-8581, JapanIn Arabidopsis the borate transporter BOR1, which is located in the plasma membrane, is degraded in the presence of excess boron by an endocytosis-mediated mechanism. A similar mechanism was suggested in rice as excess boron decreased rice borate transporter levels, although in this case whether the decrease was dependent on an increase in degradation or a decrease in protein synthesis was not elucidated. To address whether the borate-dependent degradation mechanism is conserved among plant cells, we analyzed the fate of GFP-tagged BOR1 (BOR1-GFP) in transformed tobacco BY-2 cells. Cells expressing BOR1-GFP displayed GFP fluorescence at the plasma membrane, especially at the membrane between two attached cells. The plasma membrane signal was abolished when cells were incubated in medium with a high concentration of borate (3 to 5 mM). This decrease in BOR1-GFP signal was mediated by a specific degradation of the protein after internalization by endocytosis from the plasma membrane. Pharmacological analysis indicated that the decrease in BOR1-GFP largely depends on the increase in degradation rate and that the degradation was mediated by a tyrosine-motif and the actin cytoskeleton. Tyr mutants of BOR1-GFP, which has been shown to inhibit borate-dependent degradation in Arabidopsis root cells, did not show borate-dependent endocytosis in tobacco BY-2 cells. These findings indicate that the borate-dependent degradation machinery of the borate transporter is conserved among plant species.http://f1000research.com/articles/2-185/v1Plant Biochemistry & PhysiologyPlant Cell BiologyPlant-Environment Interactions |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Noboru Yamauchi Tadashi Gosho Satoru Asatuma Kiminori Toyooka Toru Fujiwara Ken Matsuoka |
spellingShingle |
Noboru Yamauchi Tadashi Gosho Satoru Asatuma Kiminori Toyooka Toru Fujiwara Ken Matsuoka Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv] F1000Research Plant Biochemistry & Physiology Plant Cell Biology Plant-Environment Interactions |
author_facet |
Noboru Yamauchi Tadashi Gosho Satoru Asatuma Kiminori Toyooka Toru Fujiwara Ken Matsuoka |
author_sort |
Noboru Yamauchi |
title |
Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv] |
title_short |
Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv] |
title_full |
Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv] |
title_fullStr |
Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv] |
title_full_unstemmed |
Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells [v1; ref status: indexed, http://f1000r.es/kv] |
title_sort |
polarized localization and borate-dependent degradation of the arabidopsis borate transporter bor1 in tobacco by-2 cells [v1; ref status: indexed, http://f1000r.es/kv] |
publisher |
F1000 Research Ltd |
series |
F1000Research |
issn |
2046-1402 |
publishDate |
2013-09-01 |
description |
In Arabidopsis the borate transporter BOR1, which is located in the plasma membrane, is degraded in the presence of excess boron by an endocytosis-mediated mechanism. A similar mechanism was suggested in rice as excess boron decreased rice borate transporter levels, although in this case whether the decrease was dependent on an increase in degradation or a decrease in protein synthesis was not elucidated. To address whether the borate-dependent degradation mechanism is conserved among plant cells, we analyzed the fate of GFP-tagged BOR1 (BOR1-GFP) in transformed tobacco BY-2 cells. Cells expressing BOR1-GFP displayed GFP fluorescence at the plasma membrane, especially at the membrane between two attached cells. The plasma membrane signal was abolished when cells were incubated in medium with a high concentration of borate (3 to 5 mM). This decrease in BOR1-GFP signal was mediated by a specific degradation of the protein after internalization by endocytosis from the plasma membrane. Pharmacological analysis indicated that the decrease in BOR1-GFP largely depends on the increase in degradation rate and that the degradation was mediated by a tyrosine-motif and the actin cytoskeleton. Tyr mutants of BOR1-GFP, which has been shown to inhibit borate-dependent degradation in Arabidopsis root cells, did not show borate-dependent endocytosis in tobacco BY-2 cells. These findings indicate that the borate-dependent degradation machinery of the borate transporter is conserved among plant species. |
topic |
Plant Biochemistry & Physiology Plant Cell Biology Plant-Environment Interactions |
url |
http://f1000research.com/articles/2-185/v1 |
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