The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
CD40, an extracellular receptor for binding and uptake of Hsp70–peptide complexes
Open accessAbstract
Tumor and viral antigens elicit a potent immune response by heat shock protein–dependent uptake of antigenic peptide with subsequent presentation by MHC I. Receptors on antigen-presenting cells that specifically bind and internalize a heat shock protein–peptide complex have not yet been identified. Here, we show that cells expressing CD40, a cell surface protein crucial for B cell function and autoimmunity, specifically bind and internalize human Hsp70 with bound peptide. Binding of Hsp70–peptide complex to the exoplasmic domain of CD40 is mediated by the NH2-terminal nucleotide–binding domain of Hsp70 in its ADP state. The Hsp70 cochaperone Hip, but not the bacterial Hsp70 homologue DnaK, competes formation of the Hsp70–CD40 complex. Binding of Hsp70-ADP to CD40 is strongly increased in the presence of Hsp70 peptide substrate, and induces signaling via p38. We suggest that CD40 is a cochaperone-like receptor mediating the uptake of exogenous Hsp70–peptide complexes by macrophages and dendritic cells.
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Molecular characteristics of immunogenic cancer cell death
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Upadhya, R., Zingg, W., Shetty, S., & Shetty, A. K. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.04.017 · Cited by 282
Heat Shock Proteins as Endogenous Adjuvants in Sterile and Septic Inflammation
Quintana, F. J., & Cohen, I. R. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2777 · Cited by 219
Heat shock protein–based therapy as a potential candidate for treating the sphingolipidoses
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Metadata
- Authors
- Becker, T., Hartl, F.-U., & Wieland, F.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2002-09-30
- Volume
- 158
- Issue
- 7
- Pages
- 1277-1285
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2090084038
- Cited by
- 355
- References
- 33
- FWCI
- 9.94
- Type
- journal article
- Language
- en
- Open access
- green
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