TY - JOUR
T1 - Cell plate restricted association of DRP1A and PIN proteins is required for cell polarity establishment in arabidopsis
AU - Mravec, Jozef
AU - Petrášek, Jan
AU - Li, Na
AU - Boeren, Sjef
AU - Karlova, Rumyana
AU - Kitakura, Saeko
AU - Pařezová, Markéta
AU - Naramoto, Satoshi
AU - Nodzyński, Tomasz
AU - Dhonukshe, Pankaj
AU - Bednarek, Sebastian Y.
AU - Zažímalová, Eva
AU - De Vries, Sacco
AU - Friml, Jiří
N1 - Funding Information:
We thank Caterina Brancato and Vassilena Gaykova for technical assistance, European Arabidopsis Stock Centre (NASC) for providing SALK insertional lines, Martine De Cock for help in preparing the manuscript, and Herman Höfte for enabling J.M. to finalize the work in his laboratory. This work was supported by the Volkswagenstiftung (J.F. and J.M.), the Odysseus Programme of The Research Foundation—Flanders (FWO) (J.F., J.M., J.Z. and T.N.), the project of The Ministry of Education, Youth and Sports of the Czech Republic LC06034 (J.P., M.P. and E.Z.), the European Fund for Regional Development, the Operational Programme Prague—Competitiveness, project number: CZ.2.16/3.1.00/21159, the Centre for Biosystems Genomics part of the Netherlands Genomics Initiative/Netherlands Organization for Scientific Research (N.L.) and ERA-Plant Genomics (R.K.), and the Agrotechnology and Food Sciences Group of Wageningen University (S.d.V.). J.M. is indebted to the Federation of the Societies of Biochemistry and Molecular Biology (FEBS) for a long-term fellowship.
PY - 2011/6/21
Y1 - 2011/6/21
N2 - The polarized transport of the phytohormone auxin [1], which is crucial for the regulation of different stages of plant development [2, 3], depends on the asymmetric plasma membrane distribution of the PIN-FORMED (PIN) auxin efflux carriers [4, 5]. The PIN polar localization results from clathrin-mediated endocytosis (CME) from the plasma membrane and subsequent polar recycling [6]. The Arabidopsis genome encodes two groups of dynamin-related proteins (DRPs) that show homology to mammalian dynamin - a protein required for fission of endocytic vesicles during CME [7, 8]. Here we show by coimmunoprecipitation (coIP), bimolecular fluorescence complementation (BiFC), and Förster resonance energy transfer (FRET) that members of the DRP1 group closely associate with PIN proteins at the cell plate. Localization and phenotypic analysis of novel drp1 mutants revealed a requirement for DRP1 function in correct PIN distribution and in auxin-mediated development. We propose that rapid and specific internalization of PIN proteins mediated by the DRP1 proteins and the associated CME machinery from the cell plate membranes during cytokinesis is an important mechanism for proper polar PIN positioning in interphase cells.
AB - The polarized transport of the phytohormone auxin [1], which is crucial for the regulation of different stages of plant development [2, 3], depends on the asymmetric plasma membrane distribution of the PIN-FORMED (PIN) auxin efflux carriers [4, 5]. The PIN polar localization results from clathrin-mediated endocytosis (CME) from the plasma membrane and subsequent polar recycling [6]. The Arabidopsis genome encodes two groups of dynamin-related proteins (DRPs) that show homology to mammalian dynamin - a protein required for fission of endocytic vesicles during CME [7, 8]. Here we show by coimmunoprecipitation (coIP), bimolecular fluorescence complementation (BiFC), and Förster resonance energy transfer (FRET) that members of the DRP1 group closely associate with PIN proteins at the cell plate. Localization and phenotypic analysis of novel drp1 mutants revealed a requirement for DRP1 function in correct PIN distribution and in auxin-mediated development. We propose that rapid and specific internalization of PIN proteins mediated by the DRP1 proteins and the associated CME machinery from the cell plate membranes during cytokinesis is an important mechanism for proper polar PIN positioning in interphase cells.
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U2 - 10.1016/j.cub.2011.05.018
DO - 10.1016/j.cub.2011.05.018
M3 - Article
C2 - 21658946
AN - SCOPUS:79959369308
VL - 21
SP - 1055
EP - 1060
JO - Current Biology
JF - Current Biology
SN - 0960-9822
IS - 12
ER -