Journal article
The coxsackie B virus and adenovirus receptor resides in a distinct membrane microdomain
Journal of virology, Vol.77(4), pp.2559-2567
02/2003
DOI: 10.1128/JVI.77.4.2559-2567.2003
PMCID: PMC141093
PMID: 12551994
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 glycosylphosphatidylinositol (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-1-containing 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.
Details
- Title: Subtitle
- The coxsackie B virus and adenovirus receptor resides in a distinct membrane microdomain
- Creators
- Katherine J D Ashbourne Excoffon - Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USAThomas MoningerJoseph Zabner
- Resource Type
- Journal article
- Publication Details
- Journal of virology, Vol.77(4), pp.2559-2567
- DOI
- 10.1128/JVI.77.4.2559-2567.2003
- PMID
- 12551994
- PMCID
- PMC141093
- NLM abbreviation
- J Virol
- ISSN
- 0022-538X
- eISSN
- 1098-5514
- Grant note
- DK 54759 / NIDDK NIH HHS P30 DK054759 / NIDDK NIH HHS
- Language
- English
- Date published
- 02/2003
- Academic Unit
- Pulmonary, Critical Care, and Occupational Medicine; Internal Medicine
- Record Identifier
- 9984094728302771
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