| Title | Cell Membrane Lipid Rafts Mediate Caveolar Endocytosis of HIV-1 Tat Fusion Proteins |
|---|---|
| Publication Type | Articolo su Rivista peer-reviewed |
| Year of Publication | 2003 |
| Authors | Fittipaldi, A., Ferrari A., Zoppé M., Arcangeli Caterina, Pellegrini V., Beltram F., and Giacca M. |
| Journal | Journal of Biological Chemistry |
| Volume | 278 |
| Pagination | 34141-34149 |
| ISSN | 00219258 |
| Keywords | animal cell, Animalia, article, caveola, Cell Line, cell membrane, Cell membranes, Cell Nucleus, Cells, chemistry, detergent, Detergents, Endocytic pathway, endocytosis, endosome, Endosomes, Flow cytometry, fluorescence, fluorescence microscopy, gene disruption, Gene Products, Glutathione Transferase, green fluorescent protein, Green Fluorescent Proteins, HeLa cell, Hela Cells, human, human cell, Human immunodeficiency virus, Human immunodeficiency virus 1, Humans, hybrid protein, internalization, Kinetics, lipid transport, Lipids, long terminal repeat, Luminescent Proteins, Membrane Microdomains, metabolism, Microscopy, mouse, nonhuman, octoxinol, Octoxynol, photoprotein, Polymerase Chain Reaction, priority journal, protein localization, protein protein interaction, Protein Structure, protein targeting, protein tertiary structure, Proteins, signal transduction, tat, tat fusion protein, Temperature, Temperature dependence, Tertiary, Time, Time Factors, Trans-Activation (Genetics), transactivation, transactivator protein, transferrin, unclassified drug |
| Abstract | The transactivator protein of human immunodeficiency virus type 1 Tat has the unique property of mediating the delivery of large protein cargoes into the cells when present in the extracellular milieu. Here we show that Tat fusion proteins are internalized by the cells through a temperature-dependent endocytic pathway that originates from cell membrane lipid rafts and follows caveolar endocytosis. These conclusions are supported by the study of the slow kinetics of the internalization of Tat endosomes, by their resistance to nonionic detergents, the colocalization of internalized Tat with markers of caveolar endocytosis, and the impairment of the internalization process by drugs that disrupt lipid rafts or disturb caveolar trafficking. These results are of interest for all those who exploit Tat as a vehicle for transcellular protein delivery. |
| Notes | cited By 328 |
| URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141446039&doi=10.1074%2fjbc.M303045200&partnerID=40&md5=28138ab18985933b72b70ec4ce3dbebe |
| DOI | 10.1074/jbc.M303045200 |
| Citation Key | Fittipaldi200334141 |
