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| rough endoplasmic reticulum | |
|---|---|
| Name | Rough endoplasmic reticulum |
| System | Cellular organelles |
| Function | Protein synthesis, folding, quality control |
rough endoplasmic reticulum
The rough endoplasmic reticulum is a subcellular organelle characterized by membrane-bound cisternae studded with ribosomes that mediate synthesis of secretory and membrane proteins. It occupies a central position in eukaryotic secretory pathways and intersects with trafficking systems studied by researchers at institutions such as Max Planck Society, Harvard University, Massachusetts Institute of Technology, Stanford University and linked to discoveries recognized by awards like the Nobel Prize.
The morphology of the organelle is described by studies from Cambridge University, University of Oxford, Cold Spring Harbor Laboratory, European Molecular Biology Laboratory and National Institutes of Health groups that used methods developed at Bell Labs, IBM Research, GE Healthcare and Siemens. Its sheet-like cisternae and tubular networks were visualized using approaches pioneered at Howard Hughes Medical Institute and in collaborations with Wellcome Trust, Max Delbrück Center and Karolinska Institutet. Electron microscopy work influenced by teams at Rutherford Appleton Laboratory, Imperial College London, University of Tokyo and ETH Zurich revealed curvature and fenestration regulated by proteins studied in laboratories at University of California, Berkeley, Yale University, Princeton University and Columbia University.
Co-translational translation on bound ribosomes was elucidated in experiments from Rockefeller University, Johns Hopkins University, Duke University and University of Chicago that complemented biochemical frameworks developed at Salk Institute, Wistar Institute, Institute Pasteur and Max Planck Institute for Biophysical Chemistry. The coupling of translation to translocation through the translocon complex was described alongside findings from University of Cambridge, University College London, McGill University and University of Sydney investigators, while biochemical assays from Cornell University, Imperial College, University of California, San Diego and Karlsruhe Institute of Technology clarified nascent chain routing to luminal and membrane destinations.
Signal recognition particle pathway components and targeting mechanisms were characterized in landmark studies involving teams at Massachusetts General Hospital, National Cancer Institute, Fred Hutchinson Cancer Center, University of Pennsylvania and Rutgers University. Structural insights into ribosome-translocon interactions came from cryo-electron microscopy groups at European Synchrotron Radiation Facility, Diamond Light Source, Max Planck Institute for Biochemistry, University of Basel and Weizmann Institute of Science, building on genetic and biochemical work from University of Freiburg, ETH Zurich, Seoul National University and Peking University.
Glycosylation pathways and the oligosaccharyltransferase complex were elucidated by consortia including researchers at Yale School of Medicine, University of Michigan, University of Washington, Oregon Health & Science University and Monash University. The unfolded protein response and ER-associated degradation components were defined in studies from Cold Spring Harbor Laboratory, University of Toronto, Johns Hopkins University School of Medicine, University of California, San Francisco and Memorial Sloan Kettering Cancer Center, with clinical links explored by teams at Mayo Clinic, Cleveland Clinic, Massachusetts Eye and Ear, Karolinska University Hospital and Mount Sinai Health System.
Functional contacts between this organelle and mitochondria, Golgi apparatus, endosomes and plasma membrane were mapped by groups at Max Planck Institute for Molecular Cell Biology and Genetics, Barcelona Biomedical Research Park, Weizmann Institute of Science, University of Edinburgh and VIB. Tethering complexes and lipid exchange processes were studied by laboratories at University of California, Santa Cruz, Johns Hopkins Bloomberg School of Public Health, Cold Spring Harbor Laboratory, Hospital for Sick Children and University of Copenhagen, while autophagy-related interactions were explored at Institut Curie, Pasteur Institute, University of Freiburg and Technion.
Dysfunction of this organelle is implicated in hereditary disorders, metabolic diseases, neurodegeneration and cancer, topics investigated by consortia including World Health Organization, National Institutes of Health, European Research Council, Bill & Melinda Gates Foundation and clinical centers such as Massachusetts General Hospital, Johns Hopkins Hospital and Royal Free Hospital. Therapeutic strategies targeting ER stress and proteostasis pathways have been pursued in collaborations involving Pfizer, Roche, Novartis, GlaxoSmithKline and academic centers at University College London, University of Pennsylvania, Harvard Medical School and Stanford Medicine.