Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1

Research output: Contribution to journal › Journal article › Research › peer-review

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Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1. / Jørgensen, Morten Egevang; Olsen, Carl Erik; Halkier, Barbara Ann; Nour-Eldin, Hussam Hassan.

In: Plant Signalling & Behavior, Vol. 11, No. 2, e1071751, 2016.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jørgensen, ME, Olsen, CE, Halkier, BA & Nour-Eldin, HH 2016, 'Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1', Plant Signalling & Behavior, vol. 11, no. 2, e1071751. https://doi.org/10.1080/15592324.2015.1071751

APA

Jørgensen, M. E., Olsen, C. E., Halkier, B. A., & Nour-Eldin, H. H. (2016). Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1. Plant Signalling & Behavior, 11(2), [e1071751]. https://doi.org/10.1080/15592324.2015.1071751

Vancouver

Jørgensen ME, Olsen CE, Halkier BA, Nour-Eldin HH. Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1. Plant Signalling & Behavior. 2016;11(2). e1071751. https://doi.org/10.1080/15592324.2015.1071751

Author

Jørgensen, Morten Egevang ; Olsen, Carl Erik ; Halkier, Barbara Ann ; Nour-Eldin, Hussam Hassan. / Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1. In: Plant Signalling & Behavior. 2016 ; Vol. 11, No. 2.

Bibtex

@article{36ede37055a94cd3aa48eb84ab4b5213,
title = "Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1",
abstract = "Little is known about how plants regulate transporters of defense compounds. In A. thaliana, glucosinolates are transported between tissues by NPF2.10 (AtGTR1) and NPF2.11 (AtGTR2). Mining of the PhosPhat4.0 database showed two cytosol exposed phosphorylation sites for AtGTR1 and one membrane-buried phosphorylation site for AtGTR2. In this study, we investigate whether mutation of the two potential regulatory sites of AtGTR1 affected transport of glucosinolates in Xenopus oocytes. Characterization of AtGTR1 phosphorylation mutants showed that phosphorylation of AtGTR1 - at the two reported phosphorylation sites - is not directly involved in regulating AtGTR1 transport activity. We hypothesize a role for AtGTR1-phosphorylation in regulating protein-protein interactions.",
author = "J{\o}rgensen, {Morten Egevang} and Olsen, {Carl Erik} and Halkier, {Barbara Ann} and Nour-Eldin, {Hussam Hassan}",
year = "2016",
doi = "10.1080/15592324.2015.1071751",
language = "English",
volume = "11",
journal = "Plant Signalling & Behavior",
issn = "1559-2316",
publisher = "Taylor & Francis",
number = "2",

}

RIS

TY - JOUR

T1 - Phosphorylation at serine 52 and 635 does not alter the transport properties of glucosinolate transporter AtGTR1

AU - Jørgensen, Morten Egevang

AU - Olsen, Carl Erik

AU - Halkier, Barbara Ann

AU - Nour-Eldin, Hussam Hassan

PY - 2016

Y1 - 2016

N2 - Little is known about how plants regulate transporters of defense compounds. In A. thaliana, glucosinolates are transported between tissues by NPF2.10 (AtGTR1) and NPF2.11 (AtGTR2). Mining of the PhosPhat4.0 database showed two cytosol exposed phosphorylation sites for AtGTR1 and one membrane-buried phosphorylation site for AtGTR2. In this study, we investigate whether mutation of the two potential regulatory sites of AtGTR1 affected transport of glucosinolates in Xenopus oocytes. Characterization of AtGTR1 phosphorylation mutants showed that phosphorylation of AtGTR1 - at the two reported phosphorylation sites - is not directly involved in regulating AtGTR1 transport activity. We hypothesize a role for AtGTR1-phosphorylation in regulating protein-protein interactions.

AB - Little is known about how plants regulate transporters of defense compounds. In A. thaliana, glucosinolates are transported between tissues by NPF2.10 (AtGTR1) and NPF2.11 (AtGTR2). Mining of the PhosPhat4.0 database showed two cytosol exposed phosphorylation sites for AtGTR1 and one membrane-buried phosphorylation site for AtGTR2. In this study, we investigate whether mutation of the two potential regulatory sites of AtGTR1 affected transport of glucosinolates in Xenopus oocytes. Characterization of AtGTR1 phosphorylation mutants showed that phosphorylation of AtGTR1 - at the two reported phosphorylation sites - is not directly involved in regulating AtGTR1 transport activity. We hypothesize a role for AtGTR1-phosphorylation in regulating protein-protein interactions.

U2 - 10.1080/15592324.2015.1071751

DO - 10.1080/15592324.2015.1071751

M3 - Journal article

C2 - 26340317

VL - 11

JO - Plant Signalling & Behavior

JF - Plant Signalling & Behavior

SN - 1559-2316

IS - 2

M1 - e1071751

ER -

ID: 150836413