Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2003-9-1
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34141-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:12773529-Cell Line, pubmed-meshheading:12773529-Cell Membrane, pubmed-meshheading:12773529-Cell Nucleus, pubmed-meshheading:12773529-Detergents, pubmed-meshheading:12773529-Endocytosis, pubmed-meshheading:12773529-Endosomes, pubmed-meshheading:12773529-Flow Cytometry, pubmed-meshheading:12773529-Gene Products, tat, pubmed-meshheading:12773529-Glutathione Transferase, pubmed-meshheading:12773529-Green Fluorescent Proteins, pubmed-meshheading:12773529-HeLa Cells, pubmed-meshheading:12773529-Humans, pubmed-meshheading:12773529-Kinetics, pubmed-meshheading:12773529-Luminescent Proteins, pubmed-meshheading:12773529-Membrane Microdomains, pubmed-meshheading:12773529-Microscopy, Fluorescence, pubmed-meshheading:12773529-Octoxynol, pubmed-meshheading:12773529-Polymerase Chain Reaction, pubmed-meshheading:12773529-Protein Structure, Tertiary, pubmed-meshheading:12773529-Temperature, pubmed-meshheading:12773529-Time Factors, pubmed-meshheading:12773529-Transcriptional Activation, pubmed-meshheading:12773529-Transferrin
pubmed:year
2003
pubmed:articleTitle
Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 Tat fusion proteins.
pubmed:affiliation
Scuola Normale Superiore and NEST-Istituto Nazionale per la Fisica della Materia, and Istituto di Fisiologia Clinica, Consiglio Nazionale delle Ricerche, 56100 Pisa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't