Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 414151
Title Cell plate-restricted association of Arabidopsis dynamin related proteins and PIN auxin efflux carriers is required for PIN endocytic trafficking during cytokinesis.
Author(s) Mravec, J.; Petrasek, J.; Li, N.; Boeren, J.A.; Karlova, R.B.; Kitakura, S.; Naramoto, S.; Nodzynski, T.; Dhonukshe, P.B.; Vries, S.C. de; Zazimalova, E.; Friml, J.
Source Current Biology 21 (2011)12. - ISSN 0960-9822 - p. 1055 - 1060.
DOI http://dx.doi.org/10.1016/j.cub.2011.05.018
Department(s) Biochemistry
PRI BIOS Plant Development Systems
Laboratory of Molecular Biology
EPS-1
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) plant development - plasma-membrane - dynamin - auxin - endocytosis - cytokinesis - family - growth
Abstract The polarized transport of the phytohormone auxin [1], which is crucial for the regulation of different stages of plant development [ [2] and [3] ], depends on the asymmetric plasma membrane distribution of the PIN-FORMED (PIN) auxin efflux carriers [4 A. Vieten, M. Sauer, P.B. Brewer and J. Friml, Molecular and cellular aspects of auxin-transport-mediated development. Trends Plant Sci., 12 (2007), pp. 160–168. Article | PDF (558 K) | | View Record in Scopus | | Cited By in Scopus (102) [4] and [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] and [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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