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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cole, Nelson B. Donaldson, Julie G. Karabasheva, Darya |
| Description | Author Affiliation: Karabasheva D ( From the Cell Biology and Physiology Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.); Cole NB ( From the Cell Biology and Physiology Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 ncole@mail.nih.gov.); Donaldson JG ( From the Cell Biology and Physiology Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.) |
| Abstract | Proteins targeted to the plasma membrane (PM) of cells are degraded at different rates. Sorting motifs contained within the cytoplasmic domains of transmembrane proteins, post-translational modifications (e.g. ubiquitination), and assembly into multiprotein or protein-lipid complexes all may affect the efficiency of endocytosis and recycling and influence the delivery to degradative compartments. Using the SNAP-tag labeling system, we examined the turnover of a model PM protein, the chain of the interleukin-2 receptor (Tac). The surface lifetimes of SNAP-Tac fusions were influenced by their mode of entry into cells (clathrin-dependent versus clathrin-independent), their orientation in the PM (transmembrane versus glycosylphosphatidylinositol-anchored), and ubiquitination in their cytosolic domains. In addition, shedding of SNAP-Tac into the medium was greatly influenced by its O-linked glycosylation status. For a number of PM proteins, delivery to lysosomes and ectodomain shedding represent distinct parallel mechanisms to determine protein half-life. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 28 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-07-11 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Interleukin-2 Receptor Alpha Subunit Metabolism Lysosomes Models, Biological Protein Processing, Post-Translational Physiology Glycosylation HeLa Cells Genetics Isotope Labeling Protein Transport Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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