Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation

Sina Henrichs; Bangjun Wang; Yoichiro Fukao; Jinsheng Zhu; Laurence Charrier; Aurelien Bailly; Sophie C. Oehring; Miriam Linnert; Matthias Weiwad; Anne Endler; Paolo Nanni; Stephan Pollmann; Stefano Mancuso; Alexander Schulz; Markus Geisler

doi:10.1038/emboj.2012.120

Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation

Sina Henrichs, Bangjun Wang, Yoichiro Fukao, Jinsheng Zhu, Laurence Charrier, Aurelien Bailly, Sophie C. Oehring, Miriam Linnert, Matthias Weiwad, Anne Endler, Paolo Nanni, Stephan Pollmann, Stefano Mancuso, Alexander Schulz, Markus Geisler

69 Citationer (Scopus)

Abstract

Polar transport of the plant hormone auxin is controlled by PIN-and ABCB/PGP-efflux catalysts. PIN polarity is regulated by the AGC protein kinase, PINOID (PID), while ABCB activity was shown to be dependent on interaction with the FKBP42, TWISTED DWARF1 (TWD1). Using co-immunoprecipitation (co-IP) and shotgun LC-MS/MS analysis, we identified PID as a valid partner in the interaction with TWD1. In-vitro and yeast expression analyses indicated that PID specifically modulates ABCB1-mediated auxin efflux in an action that is dependent on its kinase activity and that is reverted by quercetin binding and thus inhibition of PID autophosphorylation. Triple ABCB1/PID/TWD1 co-transfection in tobacco revealed that PID enhances ABCB1-mediated auxin efflux but blocks ABCB1 in the presence of TWD1. Phospho-proteomic analyses identified S634 as a key residue of the regulatory ABCB1 linker and a very likely target of PID phosphorylation that determines both transporter drug binding and activity. In summary, we provide evidence that PID phosphorylation has a dual, counter-active impact on ABCB1 activity that is coordinated by TWD1-PID interaction.

Originalsprog	Engelsk
Tidsskrift	E M B O Journal
Vol/bind	31
Sider (fra-til)	2965-2980
Antal sider	16
ISSN	0261-4189
DOI	https://doi.org/10.1038/emboj.2012.120
Status	Udgivet - 4 jul. 2012

Adgang til dokumentet

10.1038/emboj.2012.120

Citationsformater

@article{cabd13406802415389f10123404c6007,

title = "Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation",

abstract = "Polar transport of the plant hormone auxin is controlled by PIN-and ABCB/PGP-efflux catalysts. PIN polarity is regulated by the AGC protein kinase, PINOID (PID), while ABCB activity was shown to be dependent on interaction with the FKBP42, TWISTED DWARF1 (TWD1). Using co-immunoprecipitation (co-IP) and shotgun LC-MS/MS analysis, we identified PID as a valid partner in the interaction with TWD1. In-vitro and yeast expression analyses indicated that PID specifically modulates ABCB1-mediated auxin efflux in an action that is dependent on its kinase activity and that is reverted by quercetin binding and thus inhibition of PID autophosphorylation. Triple ABCB1/PID/TWD1 co-transfection in tobacco revealed that PID enhances ABCB1-mediated auxin efflux but blocks ABCB1 in the presence of TWD1. Phospho-proteomic analyses identified S634 as a key residue of the regulatory ABCB1 linker and a very likely target of PID phosphorylation that determines both transporter drug binding and activity. In summary, we provide evidence that PID phosphorylation has a dual, counter-active impact on ABCB1 activity that is coordinated by TWD1-PID interaction.",

author = "Sina Henrichs and Bangjun Wang and Yoichiro Fukao and Jinsheng Zhu and Laurence Charrier and Aurelien Bailly and Oehring, {Sophie C.} and Miriam Linnert and Matthias Weiwad and Anne Endler and Paolo Nanni and Stephan Pollmann and Stefano Mancuso and Alexander Schulz and Markus Geisler",

year = "2012",

month = jul,

day = "4",

doi = "10.1038/emboj.2012.120",

language = "English",

volume = "31",

pages = "2965--2980",

journal = "E M B O Journal",

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TY - JOUR

T1 - Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation

AU - Henrichs, Sina

AU - Wang, Bangjun

AU - Fukao, Yoichiro

AU - Zhu, Jinsheng

AU - Charrier, Laurence

AU - Bailly, Aurelien

AU - Oehring, Sophie C.

AU - Linnert, Miriam

AU - Weiwad, Matthias

AU - Endler, Anne

AU - Nanni, Paolo

AU - Pollmann, Stephan

AU - Mancuso, Stefano

AU - Schulz, Alexander

AU - Geisler, Markus

PY - 2012/7/4

Y1 - 2012/7/4

N2 - Polar transport of the plant hormone auxin is controlled by PIN-and ABCB/PGP-efflux catalysts. PIN polarity is regulated by the AGC protein kinase, PINOID (PID), while ABCB activity was shown to be dependent on interaction with the FKBP42, TWISTED DWARF1 (TWD1). Using co-immunoprecipitation (co-IP) and shotgun LC-MS/MS analysis, we identified PID as a valid partner in the interaction with TWD1. In-vitro and yeast expression analyses indicated that PID specifically modulates ABCB1-mediated auxin efflux in an action that is dependent on its kinase activity and that is reverted by quercetin binding and thus inhibition of PID autophosphorylation. Triple ABCB1/PID/TWD1 co-transfection in tobacco revealed that PID enhances ABCB1-mediated auxin efflux but blocks ABCB1 in the presence of TWD1. Phospho-proteomic analyses identified S634 as a key residue of the regulatory ABCB1 linker and a very likely target of PID phosphorylation that determines both transporter drug binding and activity. In summary, we provide evidence that PID phosphorylation has a dual, counter-active impact on ABCB1 activity that is coordinated by TWD1-PID interaction.

AB - Polar transport of the plant hormone auxin is controlled by PIN-and ABCB/PGP-efflux catalysts. PIN polarity is regulated by the AGC protein kinase, PINOID (PID), while ABCB activity was shown to be dependent on interaction with the FKBP42, TWISTED DWARF1 (TWD1). Using co-immunoprecipitation (co-IP) and shotgun LC-MS/MS analysis, we identified PID as a valid partner in the interaction with TWD1. In-vitro and yeast expression analyses indicated that PID specifically modulates ABCB1-mediated auxin efflux in an action that is dependent on its kinase activity and that is reverted by quercetin binding and thus inhibition of PID autophosphorylation. Triple ABCB1/PID/TWD1 co-transfection in tobacco revealed that PID enhances ABCB1-mediated auxin efflux but blocks ABCB1 in the presence of TWD1. Phospho-proteomic analyses identified S634 as a key residue of the regulatory ABCB1 linker and a very likely target of PID phosphorylation that determines both transporter drug binding and activity. In summary, we provide evidence that PID phosphorylation has a dual, counter-active impact on ABCB1 activity that is coordinated by TWD1-PID interaction.

U2 - 10.1038/emboj.2012.120

DO - 10.1038/emboj.2012.120

M3 - Journal article

C2 - 22549467

SN - 0261-4189

VL - 31

SP - 2965

EP - 2980

JO - E M B O Journal

JF - E M B O Journal

ER -