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Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment （PVC） Function in Arabidopsis

Molecular Plant 2013年第6期6卷 1849-1862页

作者： Tomasz Nodzynski Mugurel I. Ferarub Sibylle Hirsch riet de rycke Claudiu Niculaes Wout Boerjan Jelle Van Leene Geert de Jaeger Steffen Vanneste Jiri Friml Mendel Centre for Plant Genomics and Proteomics Central European Institute of Technology (CEITEC) Masaryk University (MU) Kamenice 5 CZ-625 00Brno Czech Republic department of Plant Systems Biology VIB and Department of Plant Biotechnology and Bioinformatics Ghent University 9052 Gent Belgium Institute of Science and Technology Austria (IST Austria) Am Campus 1 3400 Klosterneuburg Austria Present address: department of Applied Genetics and Cell Biology University of Natural Resources and Life Sciences (BOKU) 1190 Vienna Austria Present address: Institute of Plant Biology University of Zurich 8008 ZCirich Switzerland

Intracellular protein routing is mediated by vesicular transport which is tightly regulated in eukaryotes. The protein and lipid homeostasis depends on coordinated delivery of de novo synthesized or recycled cargoes to the plasma membrane by exocytosis and their subsequent removal by rerouting them for recycling or degradation. Here, we report the characterization of protein affected trafficking 3 （pat3） mutant that we identified by an epifluorescence-based for- ward genetic screen for mutants defective in subcellular distribution of Arabidopsis auxin transporter PIN1-GFR While pat3 displays largely normal plant morphology and development in nutrient-rich conditions, it shows strong ectopic intracellular accumulations of different plasma membrane cargoes in structures that resemble prevacuolar compart- ments （PVC） with an aberrant morphology. Genetic mapping revealed that pat3 is defective in vacuolar protein sorting 35A （VPS35A）, a putative subunit of the retromer complex that mediates retrograde trafficking between the PVC and trans-Golgi network. Similarly, a mutant defective in another retromer subunit, vps29, shows comparable subcellular defects in PVC morphology and protein accumulation. Thus, our data provide evidence that the retromer components VPS35A and VPS29 are essential for normal PVC morphology and normal trafficking of plasma membrane proteins in plants. In addition, we show that, out of the three VPS35 retromer subunits present in Arabidopsis thaliana genome, the VPS35 homolog A plays a prevailing role in trafficking to the lyric vacuole, presenting another level of complexity in the retromer-dependent vacuolar sorting.

关键词： retromer VPS35 VPS29 prevacuolar compartment (PVC) vacuolar trafficking Arabidopsis thaliana.

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Repeated photoporation with graphene quantum dots enables homogeneous labeling of live cells with extrinsic markers for fluorescence microscopy

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Light(Science & Applications) 2018年第1期7卷 583-592页

作者： Jing Liu Ranhua Xiong Toon Brans Saskia Lippens Eef Parthoens Francesca Cella Zanacchi Raffaella Magrassi Santosh K.Singh Sreekumar Kurungot Sabine Szunerits Hannelore Bové Marcel Ameloot Juan C.Fraire Eline Teirlinck Sangram Keshari Samal riet de rycke Gaëlle Houthaeve Stefaan C.de Smedt Rabah Boukherroub Kevin Braeckmans Laboratory of General Biochemistry and Physical Pharmacy Faculty of PharmacyGhent UniversityGhent B-9000Belgium Centre for Nano-and Biophotonics Ghent UniversityGhent B-9000Belgium VIB-UGent Centre for Inflammation Research VIBGhent B-9000Belgium VIB Bioimaging Core VIBGhent B-9000Belgium department of Biomedical Molecular Biology Ghent UniversityGhent B-9000Belgium Nanophysics(NAPH) Istituto Italiano di TecnologiaGenova 16163Italy Biophysics Institute(IBF) National Research Council(CNR)Via De Marini6-16149–GE GenovaItaly Physical and Materials Chemistry Division CSIR-National Chemical LaboratoryDr.Homi Bhabha RoadPune 411008India Academy of Scientific and Innovative Research Anusandhan Bhawan2 RafiMargNew Delhi 110001India Univ.Lille CNRSCentrale LilleISENUniv.ValenciennesUMR 8520-IEMNLille F-59000France Biomedical Research Institute Hasselt UniversityAgoralaan Building CDiepenbeek 3590Belgium Centre for Surface Chemistry and Catalysis KU LeuvenCelestijnenlaan 200FLeuven 3001Belgium Inflammation Research Center Image Core FacilityVIB9052 GhentBelgium department of Biomedical Molecular Biology Ghent University9052 GhentBelgium department of Plant Biotechnology and Bioinformatics Ghent University9052 GentBelgium Univ Lille 1 Univ Lille Nord FranceLab Phys Lasers Atomes&MolVilleneuve Dascq UMR 852359655France College of Chemical Engineering Jiangsu Key Lab of Biomass-based Green Fuels and ChemicalsNanjing Forestry University(NFU)Nanjing 210037China UMR 8523 Laboratoire de Physique des LasersAtomes et MoléculesUniversitéde LilleVilleneuve d’AscqFrance IEMN UMR 8520Universitéde LilleVilleneuve d’AscqFrance

In the replacement of genetic probes,there is increasing interest in labeling living cells with high-quality extrinsic labels,which avoid over-expression artifacts and are available in a wide spectral *** calls for a broadly applicable technology that can deliver such labels unambiguously to the cytosol of living ***,we demonstrate that nanoparticle-sensitized photoporation can be used to this end as an emerging intracellular delivery *** replace the traditionally used gold nanoparticles with graphene nanoparticles as photothermal sensitizers to permeabilize the cell membrane upon laser *** demonstrate that the enhanced thermal stability of graphene quantum dots allows the formation of multiple vapor nanobubbles upon irradiation with short laser pulses,allowing the delivery of a variety of extrinsic cell labels efficiently and homogeneously into live *** demonstrate high-quality time-lapse imaging with confocal,total internal reflection fluorescence(TIRF),and Airyscan superresolution *** the entire procedure is readily compatible with fluorescence(super resolution)microscopy,photoporation with graphene quantum dots has the potential to become the long-awaited generic platform for controlled intracellular delivery of fluorescent labels for live-cell imaging.

关键词： quantum enable replace

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