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

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

Standard

Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation. / Henrichs, Sina; Wang, Bangjun; Fukao, Yoichiro; Zhu, Jinsheng; Charrier, Laurence; Bailly, Aurelien; Oehring, Sophie C.; Linnert, Miriam; Weiwad, Matthias; Endler, Anne; Nanni, Paolo; Pollmann, Stephan; Mancuso, Stefano; Schulz, Alexander; Geisler, Markus.

In: E M B O Journal, Vol. 31, 2012, p. 2965-2980.

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

Harvard

Henrichs, S, Wang, B, Fukao, Y, Zhu, J, Charrier, L, Bailly, A, Oehring, SC, Linnert, M, Weiwad, M, Endler, A, Nanni, P, Pollmann, S, Mancuso, S, Schulz, A & Geisler, M 2012, 'Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation', E M B O Journal, vol. 31, pp. 2965-2980. https://doi.org/10.1038/emboj.2012.120

APA

Henrichs, S., Wang, B., Fukao, Y., Zhu, J., Charrier, L., Bailly, A., Oehring, S. C., Linnert, M., Weiwad, M., Endler, A., Nanni, P., Pollmann, S., Mancuso, S., Schulz, A., & Geisler, M. (2012). Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation. E M B O Journal, 31, 2965-2980. https://doi.org/10.1038/emboj.2012.120

Vancouver

Henrichs S, Wang B, Fukao Y, Zhu J, Charrier L, Bailly A et al. Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation. E M B O Journal. 2012;31:2965-2980. https://doi.org/10.1038/emboj.2012.120

Author

Henrichs, Sina ; Wang, Bangjun ; Fukao, Yoichiro ; Zhu, Jinsheng ; Charrier, Laurence ; Bailly, Aurelien ; Oehring, Sophie C. ; Linnert, Miriam ; Weiwad, Matthias ; Endler, Anne ; Nanni, Paolo ; Pollmann, Stephan ; Mancuso, Stefano ; Schulz, Alexander ; Geisler, Markus. / Regulation of ABCB1/PGP1-catalysed auxin transport by linker phosphorylation. In: E M B O Journal. 2012 ; Vol. 31. pp. 2965-2980.

Bibtex

@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",
doi = "10.1038/emboj.2012.120",
language = "English",
volume = "31",
pages = "2965--2980",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",

}

RIS

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

Y1 - 2012

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

VL - 31

SP - 2965

EP - 2980

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

ER -

ID: 49654735