7 results on '"Łukasz Łangowski"'
Search Results
2. Cellular mechanisms for cargo delivery and polarity maintenance at different polar domains in plant cells
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Krzysztof Wabnik, Łukasz Łangowski, Satoshi Naramoto, Hirokazu Tanaka, Jiří Friml, Steffen Vanneste, and Hongjiang Li
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0301 basic medicine ,LATERAL DIFFUSION ,EFFLUX ,GNOM ARF-GEF ,Polarity (physics) ,PROTEINS ,DEPENDENT AUXIN GRADIENTS ,Endocytic recycling ,Biology ,Biochemistry ,Article ,03 medical and health sciences ,Cell polarity ,Genetics ,lateral diffusion ,Secretion ,Molecular Biology ,MEDIATES ENDOCYTOSIS ,TRANSPORTER ,Biology and Life Sciences ,protein dynamics modeling ,Cell Biology ,polar recycling ,Plant cell ,Subcellular localization ,ARABIDOPSIS ,polar secretion ,Cell biology ,580 Plants ,Multicellular organism ,030104 developmental biology ,PIN PHOSPHORYLATION ,protein clustering ,MEMBRANE TRAFFICKING ,Polar ,protein trafficking - Abstract
The asymmetric localization of proteins in the plasma membrane domains of eukaryotic cells is a fundamental manifestation of cell polarity that is central to multicellular organization and developmental patterning. In plants, the mechanisms underlying the polar localization of cargo proteins are still largely unknown and appear to be fundamentally distinct from those operating in mammals. Here, we present a systematic, quantitative comparative analysis of the polar delivery and subcellular localization of proteins that characterize distinct polar plasma membrane domains in plant cells. The combination of microscopic analyses and computational modeling revealed a mechanistic framework common to diverse polar cargos and underlying the establishment and maintenance of apical, basal, and lateral polar domains in plant cells. This mechanism depends on the polar secretion, constitutive endocytic recycling, and restricted lateral diffusion of cargos within the plasma membrane. Moreover, our observations suggest that polar cargo distribution involves the individual protein potential to form clusters within the plasma membrane and interact with the extracellular matrix. Our observations provide insights into the shared cellular mechanisms of polar cargo delivery and polarity maintenance in plant cells.
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- 2016
3. Diversification of fruit shape in the Brassicaceae family
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Łukasz Łangowski, Lars Østergaard, and Nicola Stacey
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0301 basic medicine ,Ovule ,Gynoecium ,biology ,ved/biology ,Seed dispersal ,ved/biology.organism_classification_rank.species ,Arabidopsis ,food and beverages ,Capsella ,Brassicaceae ,Cell Biology ,Plant Science ,biology.organism_classification ,Fruit morphogenesis ,03 medical and health sciences ,030104 developmental biology ,Fruit ,Capsella rubella ,Botany ,Seed Dispersal ,Morphogenesis ,Arabidopsis thaliana - Abstract
Diversity in fruit shape. Angiosperms (flowering plants) evolved during the Cretaceous Period more than 100 million years ago and quickly colonized all terrestrial habitats on the planet. A major reason for their success was the formation of fruits that would protect and nurture the developing seeds. Moreover, a massive range of diversity in fruit shape occurred during a relatively short time, which allowed for the development of ingenious ways of fertilization as well as strategies for efficient seed dispersal. The Brassicaceae family more than any exemplifies the diversity in fruit morphologies, thus providing an ideal group of plants to study how specific shapes are established. Although many genes controlling fruit patterning in the model plant Arabidopsis thaliana have been identified, the processes of carpel and fruit morphogenesis are still poorly understood. Moreover, Arabidopsis fruits are relatively simple in their structure and are therefore not ideally suited for analyzing processes of morphology determination without comparison to species with differently shaped fruits. Here, we review the diversity of fruit shape within the Brassicaceae family. As an example we describe the close relative of Arabidopsis, Capsella rubella that develops flat, heart-shaped fruits showing and highlighting its potential as a model system for research into organ shape. Recent progress in genomics including fast and cheap genome sequencing and annotation as well as development of mutant populations has opened entirely new and exciting possibilities of studying the mechanisms and processes underlying fruit formation in angiosperms.
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- 2015
4. Light-mediated polarization of the PIN3 auxin transporter for the phototropic response in Arabidopsis
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Yuanwei Fan, Jürgen Kleine-Vehn, Remko Offringa, Carlos S. Galvan-Ampudia, Emilie Demarsy, Zhaojun Ding, Łukasz Łangowski, Jiří Friml, Christian Fankhauser, Miyo Terao Morita, and Masao Tasaka
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0106 biological sciences ,Light ,Recombinant Fusion Proteins ,Arabidopsis ,01 natural sciences ,03 medical and health sciences ,Auxin ,Cell polarity ,PIN proteins ,Phototropism ,Cellular localization ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,biology ,Indoleacetic Acids ,Arabidopsis Proteins ,fungi ,Cell Polarity ,food and beverages ,Cell Biology ,biology.organism_classification ,Hypocotyl ,Cell biology ,Protein Transport ,chemistry ,Guanine nucleotide exchange factor ,Plant hormone ,010606 plant biology & botany - Abstract
Phototropism is an adaptation response, through which plants grow towards the light. It involves light perception and asymmetric distribution of the plant hormone auxin. Here we identify a crucial part of the mechanism for phototropism, revealing how light perception initiates auxin redistribution that leads to directional growth. We show that light polarizes the cellular localization of the auxin efflux carrier PIN3 in hypocotyl endodermis cells, resulting in changes in auxin distribution and differential growth. In the dark, high expression and activity of the PINOID (PID) kinase correlates with apolar targeting of PIN3 to all cell sides. Following illumination, light represses PINOID transcription and PIN3 is polarized specifically to the inner cell sides by GNOM ARF GTPase GEF (guanine nucleotide exchange factor)-dependent trafficking. Thus, differential trafficking at the shaded and illuminated hypocotyl side aligns PIN3 polarity with the light direction, and presumably redirects auxin flow towards the shaded side, where auxin promotes growth, causing hypocotyls to bend towards the light. Our results imply that PID phosphorylation-dependent recruitment of PIN proteins into distinct trafficking pathways is a mechanism to polarize auxin fluxes in response to different environmental and endogenous cues.
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- 2011
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5. Trafficking to the Outer Polar Domain Defines the Root-Soil Interface
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Jürgen Kleine-Vehn, Łukasz Łangowski, Kamil Růžička, Satoshi Naramoto, and Jiří Friml
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Recombinant Fusion Proteins ,Arabidopsis ,ATP Binding Cassette Transporter, Subfamily G ,Plant Roots ,Antiporters ,General Biochemistry, Genetics and Molecular Biology ,Soil ,Animals ,Arabidopsis thaliana ,Secretion ,Actin ,biology ,Agricultural and Biological Sciences(all) ,Arabidopsis Proteins ,Biochemistry, Genetics and Molecular Biology(all) ,Biological Transport ,Plant cell ,biology.organism_classification ,Cell biology ,Membrane ,Plant protein ,Polar ,CELLBIO ,ATP-Binding Cassette Transporters ,General Agricultural and Biological Sciences ,Function (biology) ,Signal Transduction - Abstract
Summary In animals, the interface between organism and environment is constituted by the epithelium [1]. In plants, the exchange of nutrients and signals between root and soil is crucial for their survival, but the cellular mechanisms underlying the epithelium-like function and specific localization of proteins to the root surface have not been identified [2]. Here we analyze the mechanism of polar delivery to the root-soil interface of the proteins BOR4, ABCG37, and PEN3, which transport nutrients [2], transport plant hormones, and are required for pathogen defense [3], respectively. The simultaneous visualization of these proteins and the apical and basal cargos in a single cell demonstrates that the outermost cell side represents an additional polar domain. Delivery to this outer polar domain depends on ARF GEF [4] and actin [5–8] function but does not require known molecular components of the apical or basal targeting. The outer polar delivery is, in contrast to known basal and apical cargos [9, 10], mediated by the polar secretion. Our findings show that the outermost cell membranes of roots define an additional polar domain in plant cells along with a specific, previously uncharacterized, polar targeting mechanism that is important for defining the functional, epithelium-like root-soil interface.
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- 2010
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6. Cellular and Molecular Requirements for Polar PIN Targeting and Transcytosis in Plants
- Author
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Pankaj Dhonukshe, Philip B. Brewer, Justyna Wiśniewska, Łukasz Łangowski, Jürgen Kleine-Vehn, and Jiří Friml
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Auxin efflux ,Arabidopsis ,Plant Science ,Biology ,medicine.disease_cause ,Microtubules ,Auxin ,Protein targeting ,medicine ,Guanine Nucleotide Exchange Factors ,Amino Acid Sequence ,PIN proteins ,Cytoskeleton ,Molecular Biology ,chemistry.chemical_classification ,Brefeldin A ,ADP-Ribosylation Factors ,Arabidopsis Proteins ,fungi ,Cell Polarity ,Membrane Transport Proteins ,food and beverages ,Actin cytoskeleton ,biology.organism_classification ,Actins ,Endocytosis ,Cell biology ,Protein Transport ,Transcytosis ,chemistry ,Organ Specificity - Abstract
The polar, sub-cellular localization of PIN auxin efflux carriers determines the direction of intercellular auxin flow, thus defining the spatial aspect of auxin signalling. Dynamic, transcytosis-like relocalizations of PIN proteins occur in response to external and internal signals, integrating these signals into changes in auxin distribution. Here, we examine the cellular and molecular mechanisms of polar PIN delivery and transcytosis. The mechanisms of the ARF-GEF-dependent polar targeting and transcytosis are well conserved and show little variations among diverse Arabidopsis ecotypes consistent with their fundamental importance in regulating plant development. At the cellular level, we refine previous findings on the role of the actin cytoskeleton in apical and basal PIN targeting, and identify a previously unknown role for microtubules, specifically in basal targeting. PIN protein delivery to different sides of the cell is mediated by ARF-dependent trafficking with a previously unknown complex level of distinct ARF-GEF vesicle trafficking regulators. Our data suggest that alternative recruitment of PIN proteins by these distinct pathways can account for cell type- and cargo-specific aspects of polar targeting, as well as for polarity changes in response to different signals. The resulting dynamic PIN positioning to different sides of cells defines a three-dimensional pattern of auxin fluxes within plant tissues.
- Published
- 2008
7. Recycling, clustering, and endocytosis jointly maintain PIN auxin carrier polarity at the plasma membrane
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Jiří Friml, Christian Luschnig, Łukasz Łangowski, John Runions, Satoshi Naramoto, Hirokazu Tanaka, Krzysztof Wabnik, Stefan Jakobs, Johannes Leitner, Katrin I. Willig, Willy Govaerts, Alexandre Martinière, Stéphanie Robert, Jürgen Kleine-Vehn, and Stefan W. Hell
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Stimulated Emission Depletion microscopy (STED) ,Polarity (physics) ,media_common.quotation_subject ,Arabidopsis ,Biology ,Endocytosis ,Plant Roots ,General Biochemistry, Genetics and Molecular Biology ,Exocytosis ,Article ,Diffusion ,Auxin ,Cell Wall ,Gene Expression Regulation, Plant ,trafficking ,Cell polarity ,Computer Simulation ,Internalization ,media_common ,chemistry.chemical_classification ,General Immunology and Microbiology ,Indoleacetic Acids ,Arabidopsis Proteins ,Applied Mathematics ,membrane trafficking ,Cell Membrane ,Cell Polarity ,Membrane Transport Proteins ,modeling ,systems biology ,Clathrin ,Cell biology ,Multicellular organism ,Protein Transport ,Membrane ,Computational Theory and Mathematics ,chemistry ,General Agricultural and Biological Sciences ,Information Systems - Abstract
A combination of super-resolution microscopy in live cells and computational modeling provides new insights into the dynamic and interwoven mechanism that maintains the polar distribution of an important plant cargo., Semi-quantitative and subdiffraction resolution fluorescence imaging in living plant cells provided unexpected insights into the mechanisms underlying dynamic maintenance of PIN polarity. These experiments reveal super-polar targeting of PIN proteins to the center of polar domains, presumably by a TGN/endosome guided delivery mechanism. PIN proteins are recruited to immobile membrane clusters that reduce lateral PIN mobility, and retrieved from the lateral cell side by spatially defined clathrin-dependent endocytosis. In silico model simulations are consistent with these experimental observations and reveal the individual roles of these cellular processes in the organization of sharply defined polar plasma membrane domains., Cell polarity reflected by asymmetric distribution of proteins at the plasma membrane is a fundamental feature of unicellular and multicellular organisms. It remains conceptually unclear how cell polarity is kept in cell wall-encapsulated plant cells. We have used super-resolution and semi-quantitative live-cell imaging in combination with pharmacological, genetic, and computational approaches to reveal insights into the mechanism of cell polarity maintenance in Arabidopsis thaliana. We show that polar-competent PIN transporters for the phytohormone auxin are delivered to the center of polar domains by super-polar recycling. Within the plasma membrane, PINs are recruited into non-mobile membrane clusters and their lateral diffusion is dramatically reduced, which ensures longer polar retention. At the circumventing edges of the polar domain, spatially defined internalization of escaped cargos occurs by clathrin-dependent endocytosis. Computer simulations confirm that the combination of these processes provides a robust mechanism for polarity maintenance in plant cells. Moreover, our study suggests that the regulation of lateral diffusion and spatially defined endocytosis, but not super-polar exocytosis have primary importance for PIN polarity maintenance.
- Published
- 2011
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