Lysosomal sorting mutants of coronavirus E1 protein, a Golgi membrane protein
| Autor: | S. Patel, Peter N. Riddle, J. Armstrong |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Vesicle-associated membrane protein 8
Xenopus Molecular Sequence Data Fluorescent Antibody Technique Golgi Apparatus Biology Cytoplasmic part symbols.namesake Viral Envelope Proteins Animals Amino Acid Sequence ATG16L1 Secretory pathway Murine hepatitis virus Golgi membrane Endoplasmic reticulum Biological Transport Intracellular Membranes Cell Biology COPI Golgi apparatus Biochemistry Oocytes symbols Chromosome Deletion Lysosomes |
| Zdroj: | Journal of Cell Science. 95:191-197 |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.95.2.191 |
| Popis: | As a model for the intracellular sorting of Golgi membrane proteins, we are studying the E1 protein of the coronavirus Mouse Hepatitis Virus A59. The wild-type protein, when expressed from synthetic RNA, is localised in the Golgi complex. When the second and third of the three predicted membrane-spanning sequences were deleted from the protein, the resulting mutant was retained in the endoplasmic reticulum. In contrast, removal of the first and second membrane-spanning sequences allowed the protein to pass through the Golgi complex and reach the lysosomes. Likewise, when 40 amino acids were deleted from the C-terminal cytoplasmic part of E1, the truncated protein was transported to the lysosomes. We discuss the implications of these results for the structure of the E1 protein and the mechanism by which it is localised in the cell. |
| Databáze: | OpenAIRE |
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