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  • ER  (2)
  • 1
    Keywords: CELLS ; CELL ; Germany ; screening ; SYSTEM ; PROTEIN ; PROTEINS ; SAMPLE ; COMPLEX ; COMPLEXES ; TRANSPORT ; ACQUISITION ; ASSAY ; TRAFFICKING ; LOCALIZATION ; ER ; green fluorescent protein,proteomics,functional analysis,high-content screening microscopy,membrane ; MANAGEMENT
    Abstract: A modular microscope-based screening platform, with applications in large-scale analysis of protein function in intact cells is described. It includes automated sample preparation, image acquisition, data management and analysis, and the genome-wide automated retrieval of bioinformatic information. The modular nature of the system ensures that it is rapidly adaptable to new biological questions or sets of proteins. Two automated functional assays addressing protein secretion and the integrity of the Golgi complex were developed and tested. This shows the potential of the system in large-scale, cell-based functional proteomic projects. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 14623100
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  • 2
    Keywords: CELLS ; CELL ; Germany ; human ; MICROSCOPY ; PATHWAY ; screening ; PROTEIN ; PROTEINS ; COMPLEX ; COMPLEXES ; DOMAIN ; TRANSPORT ; YEAST ; ASSAY ; MEMBRANE ; HUMAN GENOME ; GOLGI-APPARATUS ; MORPHOLOGY ; FUTURE ; ESTABLISHMENT ; REGULATOR ; REGULATORS ; DOMAINS ; ENDOPLASMIC-RETICULUM ; ER ; SUBCELLULAR-LOCALIZATION ; coiled coil ; COILED-COIL ; COPII ; MATRIX PROTEINS
    Abstract: Here we describe the establishment of microscope-based functional screening assays in intact cells that allow LIS to systematically identify new proteins involved in secretory membrane traffic, and proteins that can influence the integrity of the Golgi complex. We were able to identify 20 new proteins that affected either secretory transport, Golgi morphology, or both, when overexpressed in cells. Control experiments with human orthologs to yeast proteins with a role in membrane traffic, or already well characterized mammalian regulators of the secretory pathway, confirmed the specificity and significance of our results. Proteins localized to the Golgi complex or endoplasmic reticulum (ER) showed preferential interference in Our assays. Bioinformatic analysis of the new proteins interfering with membrane traffic and/or Golgi integrity revealed broad functional variety, but demonstrated a bias towards proteins with predicted coiled-coil domains and repeat structures. Extending our approach to a much larger set of novel proteins in the future will be an important step toward a more comprehensive understanding of the molecular basis of the secretory pathway. It will also serve as an example for similar microscope-based screens addressing different biological questions
    Type of Publication: Journal article published
    PubMed ID: 15466293
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