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TWISTED DWARF1 mediates the action of auxin transport inhibitors on actin cytoskeleton dynamics

  • Zhu, Jinsheng Department of Biology, University of Fribourg, Switzerland - Structural Plant Biology Laboratory, Department of Botany and Plant Biology, Geneva, Switzerland
  • Bailly, Aurelien Department of Biology, University of Fribourg, Switzerland - Department of Plant and Microbial Biology, University of Zurich, Switzerland
  • Zwiewka, Marta CEITEC-Central European Institute of Technology, Masaryk University, Brno, Czech Republic
  • Sovero, Valpuri Department of Plant and Microbial Biology, University of Zurich, Switzerland
  • Donato, Martin Di Department of Biology, University of Fribourg, Switzerland
  • Ge, Pei Department of Biology, University of Fribourg, Switzerland - Station Biologique de Roscoff, CNRS-UPMC, France
  • Oehri, Jacqueline Department of Biology, University of Fribourg, Switzerland - Institute of Evolutionary Biology and Environmental Studies, University of Zurich, Switzerland
  • Aryal, Bibek Department of Biology, University of Fribourg, Switzerland
  • Hao, Pengchao Department of Biology, University of Fribourg, Switzerland
  • Linnert, Miriam Max Planck Research Unit for Enzymology of Protein Folding, Halle (Saale), Germany - Faunhofer Institute for Cell Therapy and Immunology IZI, Department of Drug Design and Target Validation, Halle, Germany
  • Burgardt, Noelia Inés Max Planck Research Unit for Enzymology of Protein Folding, Halle (Saale), Germany - Institute of Biochemistry and Biophysics (IQUIFIB), School of Pharmacy and Biochemistry, University of Buenos Aires, Argentina
  • Lücke, Christian Max Planck Research Unit for Enzymology of Protein Folding, Halle (Saale), Germany
  • Weiwad, Matthias Max Planck Research Unit for Enzymology of Protein Folding, Halle (Saale), Germany - Department of Enzymology, Martin-Luther-University Halle-Wittenberg, Institute of Biochemistry and Biotechnology, Halle, Germany
  • Michel, Max Institute of Complex Systems, ICS-6: Structural Biochemistry, Jülich, Germany
  • Weiergräber, Oliver H. Institute of Complex Systems, ICS-6: Structural Biochemistry, Jülich, Germany
  • Pollmann, Stephan Centro de Biotecnología y Genómica de Plantas, Pozuelo de Alarcón, Madrid, Spain
  • Azzarello, Elisa LINV-DIPSAA, Università di Firenze, Italy
  • Mancuso, Stefano LINV-DIPSAA, Università di Firenze, Italy
  • Ferro, Noel University of Bonn, Mulliken Center for Theoretical Chemistry, Institute for Physical and Theoretical Chemistry, Bonn, Germany
  • Fukao, Yoichiro Plant Global Educational Project, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Japan - Department of Bioinfomatics, Ritsumeikan University, Shiga, Japan
  • Hoffmann, Céline Cytoskeleton and Cancer Progression, Laboratory of Experimental Cancer Research, Department of Oncology, Luxembourg Institute of Health, Luxembourg
  • Wedlich-Söldner, Roland Institute of Cell Dynamics and Imaging, University of Münster, Germany
  • Friml, Jiří Institute of Science and Technology, Klosterneuburg, Austria
  • Thomas, Clément Cytoskeleton and Cancer Progression, Laboratory of Experimental Cancer Research, Department of Oncology, Luxembourg Institute of Health, Luxembourg
  • Geisler, Markus Department of Biology, University of Fribourg, Switzerland - Department of Plant and Microbial Biology, University of Zurich, Switzerland
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    01.04.2016
Published in:
  • The Plant Cell. - 2016, vol. 28, no. 4, p. 930–948
English Plant growth and architecture is regulated by the polar distribution of the hormone auxin. Polarity and flexibility of this process is provided by constant cycling of auxin transporter vesicles along actin filaments, coordinated by a positive auxin-actin feedback loop. Both polar auxin transport and vesicle cycling are inhibited by synthetic auxin transport inhibitors, such as 1-N-naphthylphthalamic acid (NPA), counteracting the effect of auxin; however, underlying targets and mechanisms are unclear. Using NMR, we map the NPA binding surface on the Arabidopsis thaliana ABCB chaperone TWISTED DWARF1 (TWD1). We identify ACTIN7 as a relevant, although likely indirect, TWD1 interactor, and show TWD1-dependent regulation of actin filament organization and dynamics and that TWD1 is required for NPA-mediated actin cytoskeleton remodeling. The TWD1-ACTIN7 axis controls plasma membrane presence of efflux transporters, and as a consequence act7 and twd1 share developmental and physiological phenotypes indicative of defects in auxin transport. These can be phenocopied by NPA treatment or by chemical actin (de)stabilization. We provide evidence that TWD1 determines downstream locations of auxin efflux transporters by adjusting actin filament debundling and dynamizing processes and mediating NPA action on the latter. This function appears to be evolutionary conserved since TWD1 expression in budding yeast alters actin polarization and cell polarity and provides NPA sensitivity.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biological sciences
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/304933
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Supplementary material
Supplementary material
pool Co-IP 1- subtracted Col Wt
pool Co-IP 1- subtracted Col Wt
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pool co-IP1-3 subtracted all Co
pool co-IP1-3 subtracted all Co
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