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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eraa212
|2 doi
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|a pubmed24n1035.xml
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|a (DE-627)NLM310645239
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|a (NLM)32484219
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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 |
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|a Lara, Alberto
|e verfasserin
|4 aut
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| 245 |
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|a Arabidopsis K+ transporter HAK5-mediated high-affinity root K+ uptake is regulated by protein kinases CIPK1 and CIPK9
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|c 2020
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 14.05.2021
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| 500 |
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|a Date Revised 31.05.2022
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a The high-affinity K+ transporter HAK5 is the major contributor to root K+ uptake from dilute solutions in K+-starved Arabidopsis plants. Its functionality is tightly regulated and its activity is enhanced under K+ starvation by the transcriptional induction of the AtHAK5 gene, and by the activation of the transporter via the AtCBL1-AtCIPK23 complex. In the present study, the 26 members of the Arabidopsis CIPK protein kinase family were screened in yeast for their capacity to activate HAK5-mediated K+ uptake. Among them, AtCIPK1 was the most efficient activator of AtHAK5. In addition, AtCIPK9, previously reported to participate in K+ homeostasis, also activated the transporter. In roots, the genes encoding AtCIPK1 and AtCIPK9 were induced by K+ deprivation and atcipk1 and atcipk9 Arabidopsis KO mutants showed a reduced AtHAK5-mediated Rb+ uptake. Activation of AtHAK5 by AtCIPK1 did not occur under hyperosmotic stress conditions, where AtCIPK1 function has been shown to be required to maintain plant growth. Taken together, our data contribute to the identification of the complex regulatory networks that control the high-affinity K+ transporter AtHAK5 and root K+ uptake
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Arabidopsis
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|a AtCBL
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|a AtCIPK
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|a AtHAK5
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|a potassium
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|a uptake
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|a Arabidopsis Proteins
|2 NLM
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|a Potassium Channels
|2 NLM
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| 650 |
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|a Potassium-Hydrogen Antiporters
|2 NLM
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| 650 |
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|a Symporters
|2 NLM
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| 650 |
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|a Protein Kinases
|2 NLM
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| 650 |
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|a EC 2.7.-
|2 NLM
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| 650 |
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|a CIPK1 protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 2.7.11.1
|2 NLM
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| 650 |
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|a CIPK9 protein, Arabidopsis
|2 NLM
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| 650 |
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7 |
|a EC 2.7.11.1
|2 NLM
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| 650 |
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|a Protein Serine-Threonine Kinases
|2 NLM
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| 650 |
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|a EC 2.7.11.1
|2 NLM
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| 650 |
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|a Potassium
|2 NLM
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| 650 |
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7 |
|a RWP5GA015D
|2 NLM
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| 700 |
1 |
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|a Ródenas, Reyes
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Andrés, Zaida
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Martínez, Vicente
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Quintero, Francisco J
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Nieves-Cordones, Manuel
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Botella, M Angeles
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Rubio, Francisco
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 71(2020), 16 vom: 06. Aug., Seite 5053-5060
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:71
|g year:2020
|g number:16
|g day:06
|g month:08
|g pages:5053-5060
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| 856 |
4 |
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|u http://dx.doi.org/10.1093/jxb/eraa212
|3 Volltext
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|a AR
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|d 71
|j 2020
|e 16
|b 06
|c 08
|h 5053-5060
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