| Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein. | |
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MedLine Citation:
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PMID: 11867532 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The human cytomegalovirus gene products US2 and US11 induce proteasomal degradation of MHC class I heavy chains. We have generated an enhanced green fluorescent protein-class I heavy chain (EGFP-HC) chimeric molecule to study its dislocation and degradation in US2- and US11-expressing cells. The EGFP-HC fusion is stable in control cells, but is degraded rapidly in US2- or US11-expressing cells. Proteasome inhibitors induce in a time-dependent manner the accumulation of EGFP-HC molecules in US2- and US11-expressing cells, as assessed biochemically and by cytofluorimetry of intact cells. Pulse-chase analysis and subcellular fractionation show that EGFP-HC proteins are dislocated from the endoplasmic reticulum and can be recovered as deglycosylated fluorescent intermediates in the cytosol. These results raise the possibility that dislocation of glycoproteins from the ER may not require their full unfolding. |
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Authors:
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Edda Fiebiger; Craig Story; Hidde L Ploegh; Domenico Tortorella |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The EMBO journal Volume: 21 ISSN: 0261-4189 ISO Abbreviation: EMBO J. Publication Date: 2002 Mar |
Date Detail:
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Created Date: 2002-02-27 Completed Date: 2002-05-14 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: England |
Other Details:
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Languages: eng Pagination: 1041-53 Citation Subset: IM |
Affiliation:
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Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Armenise Building, Boston, MA 02115, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Astrocytoma / pathology Brain Neoplasms / pathology Cysteine Endopeptidases / metabolism Cytomegalovirus / genetics Cytosol / metabolism* Endoplasmic Reticulum / metabolism* Flow Cytometry Genes, Synthetic Glycosylation Green Fluorescent Proteins H-2 Antigens / genetics, metabolism* HLA-A2 Antigen / genetics, metabolism* Humans Luminescent Proteins / genetics, metabolism Membrane Glycoproteins / metabolism* Mice Multienzyme Complexes / metabolism Peptide Fragments / genetics, metabolism Proteasome Endopeptidase Complex Protein Folding Protein Processing, Post-Translational Protein Sorting Signals / genetics, physiology Protein Transport* RNA-Binding Proteins / genetics, metabolism Recombinant Fusion Proteins / genetics, metabolism Subcellular Fractions / chemistry Transfection Tumor Cells, Cultured Viral Envelope Proteins / genetics, metabolism Viral Proteins / genetics, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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5R37-AI33456/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/H-2 Antigens; 0/H-2Kb protein, mouse; 0/HLA-A2 Antigen; 0/Luminescent Proteins; 0/Membrane Glycoproteins; 0/Multienzyme Complexes; 0/Peptide Fragments; 0/Protein Sorting Signals; 0/RNA-Binding Proteins; 0/Recombinant Fusion Proteins; 0/US11 protein, herpesvirus; 0/US2 protein, Varicellovirus; 0/Viral Envelope Proteins; 0/Viral Proteins; 147336-22-9/Green Fluorescent Proteins; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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