The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Cell surface adherence and endocytosis of protein transduction domains
Open accessAbstract
Protein transduction domains (PTD), such as the HIV TAT and the herpes simplex virus VP22 proteins, are reported to translocate across the membranes of mammalian cells. The mechanism of PTD membrane translocation has largely remained elusive, but recent studies suggest that the reported PTD translocation is due to a fixation artifact. We have constructed and expressed the PTDs VP22, TAT, polyarginine, and polylysine fused to the green fluorescent protein to visualize these proteins in both living and fixed cells. The investigated PTDs strongly adhered to the surface of living cells and were internalized by constitutive endocytosis. No cytosolic or nuclear import of the proteins was detected. In contrast, the PTD-GFP fusion proteins were redistributed to the cytosol and nucleus directly after fixation. Our findings suggest that the PTDs only mediate cell surface adherence, a property shared with many other positively charged macromolecules. The cell surface adherence results in endocytosis and accumulation of proteins in endosomes. We suggest that the biological effects observed for PTD fusion proteins are due to cell surface interactions and internalization of the proteins into cells by classical endocytosis.
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Cites
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Cited by
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Uptake Pathways and Subsequent Intracellular Trafficking in Nonviral Gene Delivery
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CNS Delivery Via Adsorptive Transcytosis
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Tat peptide-mediated cellular delivery: back to basics
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Metadata
- Authors
- Lundberg, M., Wikström, S., & Johansson, M.
- Venue
- Molecular Therapy
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 8
- Issue
- 1
- Pages
- 143-150
- ISSN
- 1525-0016 (ISSN-L)
- OpenAlex
- W1996805840
- Cited by
- 301
- References
- 39
- FWCI
- 10.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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