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

Morten Egevang Jørgensen; Carl Erik Olsen; Barbara Ann Halkier; Hussam Hassan Nour-Eldin

doi:10.1080/15592324.2015.1071751

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

Morten Egevang Jørgensen, Carl Erik Olsen, Barbara Ann Halkier, Hussam Hassan Nour-Eldin

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.

Originalsprog	Engelsk
Artikelnummer	e1071751
Tidsskrift	Plant Signalling & Behavior
Vol/bind	11
Udgave nummer	2
Antal sider	6
ISSN	1559-2316
DOI	https://doi.org/10.1080/15592324.2015.1071751
Status	Udgivet - 1 feb. 2016

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10.1080/15592324.2015.1071751

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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.",

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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 - 2016/2/1

Y1 - 2016/2/1

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

SN - 1559-2316

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JO - Plant Signalling & Behavior

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

Abstract

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