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The Coxsackie B Virus and Adenovirus Receptor Resides in a Distinct Membrane Microdomain.
- Source :
-
Journal of Virology . Feb2003, Vol. 77 Issue 4, p2559. 9p. 4 Diagrams, 3 Graphs. - Publication Year :
- 2003
-
Abstract
- The coxsackie B virus and adenovirus receptor (CAR) is a member of the immunoglobulin superfamily. In addition to activity as a viral receptor, it may play a role in cellular adhesion. We asked what determines the cell membrane microdomain of CAR. We found that CAR is localized to a novel lipid-rich microdomain similar to that of the low-density lipoprotein receptor (LDLR) but distinct from that of a CAR variant that exhibited traditional lipid raft localization via fusion to a glycosylphosphatidylinositoi (GPI) tail. The cytoplasmic tail determines its membrane localization, since deletion of this domain resulted in mislocalization. Results indicate that CAR, CAR-LDLR, and LDLR reside in a novel lipid raft that is distinct from caveolin-1containing caveolae and GPI-linked proteins. Residence in a lipid-rich domain provides a mechanism that allows CAR to interact with other cell adhesion proteins and yet function as an adenovirus receptor. [ABSTRACT FROM AUTHOR]
- Subjects :
- *COXSACKIEVIRUSES
*ADENOVIRUSES
Subjects
Details
- Language :
- English
- ISSN :
- 0022538X
- Volume :
- 77
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- Journal of Virology
- Publication Type :
- Academic Journal
- Accession number :
- 10306355
- Full Text :
- https://doi.org/10.1128/JVI.77.4.2559-2567.2003