Journal article
The CD20 calcium channel is localized to microvilli and constitutively associated with membrane rafts: antibody binding increases the affinity of the association through an epitope-dependent cross-linking-independent mechanism
The Journal of biological chemistry, v 279(19), pp 19893-19901
07 May 2004
PMID: 14976189
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
CD20 is a B cell-specific membrane protein that functions in store-operated calcium entry and serves as a useful target for antibody-mediated therapeutic depletion of B cells. Antibody binding to CD20 induces a diversity of biological effects, some of which are dependent on lipid rafts. Rafts are isolated as low density detergent-resistant membranes, initially characterized using Triton X-100. We have previously reported that CD20 is soluble in 1% Triton but that antibodies induce the association of CD20 with Triton-resistant rafts. However, by using several other detergents to isolate rafts and by microscopic co-localization with a glycosylphosphatidylinositol-linked protein, we show in this report that CD20 is constitutively raft-associated. CD20 was distributed in a punctate pattern on the cell surface as visualized by fluorescence imaging and was also localized to microvilli by electron microscopy. The mechanism underlying antibody-induced association of CD20 with Triton-resistant rafts was investigated and found not to require cellular ATP, kinase activity, actin polymerization, or antibody cross-linking but was dependent on the epitope recognized. Thus, antibody-induced insolubility in 1% Triton most likely reflects a transition from relatively weak to strong raft association that occurs as a result of a conformational change in the CD20 protein.
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Details
- Title
- The CD20 calcium channel is localized to microvilli and constitutively associated with membrane rafts: antibody binding increases the affinity of the association through an epitope-dependent cross-linking-independent mechanism
- Creators
- Haidong Li - University of CalgaryLinda M Ayer - University of CalgaryMaria J Polyak - University of CalgaryCathlin M Mutch - University of CalgaryRyan J Petrie - University of CalgaryLaura Gauthier - University of CalgaryNeda Shariat - University of CalgaryMichael J Hendzel - University of AlbertaAndrew R ShawKamala D Patel - University of CalgaryJulie P Deans - University of Calgary
- Publication Details
- The Journal of biological chemistry, v 279(19), pp 19893-19901
- Publisher
- ASBMB Publications / Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000221164500063
- Scopus ID
- 2-s2.0-2442522360
- Other Identifier
- 991020100192804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology