Forced degradation of Fas inhibits apoptosis in adenovirus-infected cells

Ann E. Tollefson, Terry W. Hermiston, Drew L. Lichtenstein, Clarence F. Colle, Ralph A. Tripp, Todor Dimitrov, Karoly Toth, Christopher E. Wells, Peter C. Doherty and William S. M. Wold ()
Additional contact information
Ann E. Tollefson: St Louis University School of Medicine
Terry W. Hermiston: St Louis University School of Medicine
Drew L. Lichtenstein: St Louis University School of Medicine
Clarence F. Colle: St Louis University School of Medicine
Ralph A. Tripp: St Jude Children's Research Hospital
Todor Dimitrov: St Louis University School of Medicine
Karoly Toth: St Louis University School of Medicine
Christopher E. Wells: St Louis University School of Medicine
Peter C. Doherty: St Jude Children's Research Hospital
William S. M. Wold: St Louis University School of Medicine

Nature, 1998, vol. 392, issue 6677, 726-730

Abstract: Abstract DNA viruses have evolved elaborate mechanisms to overcome host antiviral defences. In adenovirus-infected cells, programmed cell death (apoptosis) induced by the cytokine tumour necrosis factor (TNF) is inhibited by several adenovirus-encoded proteins1,2,3. Occupation of the cell-surface receptor Fas, a member of the TNF-receptor superfamily that is expressed on most cell types, triggers apoptosis of that cell4,5,6. Here we show that the adenovirus RID (for receptor internalization and degradation) protein complex, which is an inhibitor of TNF-induced apoptosis2, mediates internalization of cell-surface Fas and its destruction inside lysosomes within the cell. Fas has not previously been shown to be internalized and then degraded. RID also mediates internalization of the receptor for epidermal growth factor7,8, but it does not affect the transferrin receptor or class I antigens of the major histocompatibility complex. Removal of Fas from the surface of adenovirus-infected cells expressing RID may allow infected cells to resist Fas-mediated cell death and thus promote their survival.

Date: 1998
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/33712 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:392:y:1998:i:6677:d:10.1038_33712

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/33712

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().