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Auxin-transporting ABC transporters are defined by a conserved D/E-P motif regulated by a prolylisomerase

  • Hao, Pengchao Department of Biology, University of Fribourg, Fribourg, Switzerland
  • Xia, Jian Department of Biology, University of Fribourg, Fribourg, Switzerland
  • Liu, Jie Department of Biology, University of Fribourg, Fribourg, Switzerland
  • Donato, Martin Di Department of Biology, University of Fribourg, Fribourg, Switzerland
  • Pakula, Konrad Department of Plant Molecular Physiology, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland - NanoBioMedical Centre, Adam Mickiewicz University, Poznan, Poland
  • Bailly, Aurélien Institute for Plant and Microbial Biology, Zurich, Switzerland
  • Jasinski, Michal Department of Plant Molecular Physiology, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland - Department of Biochemistry and Biotechnology, Poznan University of Life Sciences, Poznan, Poland
  • Geisler, Markus Department of Biology, University of Fribourg, Fribourg, Switzerland
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    11.09.2020
Published in:
  • Journal of Biological Chemistry. - 2020, vol. 295, no. 37, p. 13094–13105
English The plant hormone auxin must be transported throughout plants in a cell-to-cell manner to affect its various physiological functions. ABCB transporters are critical for this polar auxin distribution, but the regulatory mechanisms controlling their function is not fully understood. The auxin transport activity of ABCB1 was suggested to be regulated by a physical interaction with FKBP42/Twisted Dwarf1 (TWD1), a peptidylprolyl cis-trans isomerase (PPIase), but all attempts to demonstrate such a PPIase activity by TWD1 have failed so far. By using a structure-based approach, we identified several surface-exposed proline residues in the nucleotide binding domain and linker of Arabidopsis ABCB1, mutations of which do not alter ABCB1 protein stability or location but do affect its transport activity. P1008 is part of a conserved signature D/E-P motif that seems to be specific for auxin-transporting ABCBs, which we now refer to as ATAs. Mutation of the acidic residue also abolishes auxin transport activity by ABCB1. All higher plant ABCBs for which auxin transport has been conclusively proven carry this conserved motif, underlining its predictive potential. Introduction of this D/E-P motif into malate importer, ABCB14, increases both its malate and its background auxin transport activity, suggesting that this motif has an impact on transport capacity. The D/E-P1008 motif is also important for ABCB1-TWD1 interactions and activation of ABCB1-mediated auxin transport by TWD1. In summary, our data imply a new function for TWD1 acting as a putative activator of ABCB- mediated auxin transport by cis-trans isomerization of peptidyl-prolyl bonds.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biology
License
License undefined
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Persistent URL
https://folia.unifr.ch/unifr/documents/309053
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