Cell Membrane Lipid Rafts Mediate Caveolar Endocytosis of HIV-1 Tat Fusion Proteins*
By Antonio Fittipaldi, A. Ferrari, M. Zoppè, C. Arcangeli, V. Pellegrini, F. Beltram, M. Giacca. Journal of Biological Chemistry, 2003
245 citations recorded by the source corpus.
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.
Subfields: Molecular Biology, Virology
View Paper: https://www.semanticscholar.org/paper/0284b489b64216fcee41fd32936990d8c301edf7
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Citations in the corpus
- Cellular uptake of arginine-rich peptides: roles for macropinocytosis and actin rearrangement. (2004, background): “Several endocytic routes have been suggested for the cellular uptake of Tat and other arginine peptides [7,19– 21,32].”
- CNS Delivery Via Adsorptive Transcytosis (2008, methodology): “In fact, later studies have shown that CPP translocation is mostly a temperature-dependent process (53) and have established the possible role of endocytosis in the internalization of CPPs (52,54, 55 ).”