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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erz230
|2 doi
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|a pubmed24n0990.xml
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|a (DE-627)NLM297058851
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|a (NLM)31087098
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Wu, Xiangyu
|e verfasserin
|4 aut
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| 245 |
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|a Ammonium and nitrate regulate NH4+ uptake activity of Arabidopsis ammonium transporter AtAMT1;3 via phosphorylation at multiple C-terminal sites
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 27.07.2020
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|a Date Revised 27.07.2020
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a In plants, nutrient transporters require tight regulation to ensure optimal uptake in complex environments. The activities of many nutrient transporters are post-translationally regulated by reversible phosphorylation, allowing rapid adaptation to variable environmental conditions. Here, we show that the Arabidopsis root epidermis-expressed ammonium transporter AtAMT1;3 was dynamically (de-)phosphorylated at multiple sites in the cytosolic C-terminal region (CTR) responding to ammonium and nitrate signals. Under ammonium resupply rapid phosphorylation of a Thr residue (T464) in the conserved part of the CTR (CTRC) effectively inhibited AtAMT1;3-dependent NH4+ uptake. Moreover, phosphorylation of Thr (T494), one of three phosphorylation sites in the non-conserved part of the CTR (CRTNC), moderately decreased the NH4+ transport activity of AtAMT1;3, as deduced from functional analysis of phospho-mimic mutants in yeast, oocytes, and transgenic Arabidopsis. Double phospho-mutants indicated a role of T494 in fine-tuning the NH4+ transport activity when T464 was non-phosphorylated. Transient dephosphorylation of T494 with nitrate resupply closely paralleled a transient increase in ammonium uptake. These results suggest that T464 phosphorylation at the CTRC acts as a prime switch to prevent excess ammonium influx, while T494 phosphorylation at the CTRNC fine tunes ammonium uptake in response to nitrate. This provides a sophisticated regulatory mechanism for plant ammonium transporters to achieve optimal ammonium uptake in response to various nitrogen forms
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Ammonium transporter (AMT)
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|a ammonium uptake
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|a membrane transport
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|a multisite phosphorylation
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| 650 |
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|a nitrogen signals
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|a phosphorylation
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|a post-translational regulation
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| 650 |
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|a Ammonium Compounds
|2 NLM
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| 650 |
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|a Cation Transport Proteins
|2 NLM
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| 650 |
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|a Nitrates
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a ammonium transporters, plant
|2 NLM
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| 700 |
1 |
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|a Liu, Ting
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Yongjian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Duan, Fengying
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Neuhäuser, Benjamin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ludewig, Uwe
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schulze, Waltraud X
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yuan, Lixing
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 70(2019), 18 vom: 24. Sept., Seite 4919-4930
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:70
|g year:2019
|g number:18
|g day:24
|g month:09
|g pages:4919-4930
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/erz230
|3 Volltext
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|d 70
|j 2019
|e 18
|b 24
|c 09
|h 4919-4930
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