Arabidopsis thaliana MRP1 (AtABCC1) nucleotide binding domain contributes to arsenic stress tolerance with serine triad phosphorylation

Copyright © 2016 Elsevier Masson SAS. All rights reserved.

Détails bibliographiques
Publié dans:Plant physiology and biochemistry : PPB. - 1991. - 108(2016) vom: 03. Nov., Seite 109-120
Auteur principal: Raichaudhuri, Ayan (Auteur)
Format: Article en ligne
Langue:English
Publié: 2016
Accès à la collection:Plant physiology and biochemistry : PPB
Sujets:Journal Article ABC transporter Arabidopsis thaliana Arsenic stress Phosphorylation Serine triad ABCC1 protein, Arabidopsis ATP-Binding Cassette Transporters Arabidopsis Proteins Arsenites plus... Folic Acid Antagonists Serine 452VLY9402 Casein Kinase II EC 2.7.11.1 arsenite N5509X556J Arsenic N712M78A8G Methotrexate YL5FZ2Y5U1
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245 1 0 |a Arabidopsis thaliana MRP1 (AtABCC1) nucleotide binding domain contributes to arsenic stress tolerance with serine triad phosphorylation 
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520 |a Copyright © 2016 Elsevier Masson SAS. All rights reserved. 
520 |a Multidrug resistance protein AtMRPs belong to the ATP binding cassette (ABC) transporter super family. ABC proteins are membrane proteins involved in the transport of a broad range of amphipathic organic anions across membranes. MRPs (ABCCs) are one of the highly represented subfamilies of ABC transporters. Plant MRPs also transport various glutathione conjugates across membranes. Arabidopsis thaliana MRP1 is already known to be involved in vacuolar storage of folates. Using heterologously expressed AtMRP1 in yeast and its C-terminal nucleotide binding domain (NBD2) in Escherichia coli, it has been shown that Casein kinase II (CKII) mediated phosphorylation is a potential regulator of AtMRP1 function. AtMRP1 showed enhanced tolerance towards arsenite As(III) in yeast. CKIIII/CKII mediated phosphorylation of AtMRP1 was found to be involved in As(III) mediated signaling. AtMRP1-NBD2 and its serine mutants showed distinct change in secondary structure in the presence of arsenite and methotrexate (MTX) controlled by serine triad phosphorylation. Results showed that AtMRP1 is important for vacuolar accumulation of antifolates as well as tolerance against arsenic, both of which involved phosphorylation in the serine triads at the C terminal NBD of AtMRP1. The experiments provide an important insight into the role of AtMRP1 serine triad phosphorylation under AsIII stress conditions 
650 4 |a Journal Article 
650 4 |a ABC transporter 
650 4 |a Arabidopsis thaliana 
650 4 |a Arsenic stress 
650 4 |a Phosphorylation 
650 4 |a Serine triad 
650 7 |a ABCC1 protein, Arabidopsis  |2 NLM 
650 7 |a ATP-Binding Cassette Transporters  |2 NLM 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Arsenites  |2 NLM 
650 7 |a Folic Acid Antagonists  |2 NLM 
650 7 |a Serine  |2 NLM 
650 7 |a 452VLY9402  |2 NLM 
650 7 |a Casein Kinase II  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a arsenite  |2 NLM 
650 7 |a N5509X556J  |2 NLM 
650 7 |a Arsenic  |2 NLM 
650 7 |a N712M78A8G  |2 NLM 
650 7 |a Methotrexate  |2 NLM 
650 7 |a YL5FZ2Y5U1  |2 NLM 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 108(2016) vom: 03. Nov., Seite 109-120  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:108  |g year:2016  |g day:03  |g month:11  |g pages:109-120 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2016.07.005  |3 Volltext 
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