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- Title
Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics.
- Authors
Gupta, Neetu; Wollscheid, Bernd; Watts, Julian D; Scheer, Barbara; Aebersold, Ruedi; DeFranco, Anthony L
- Abstract
Ligation of the B cell antigen receptor (BCR) with antigen induces lipid raft coalescence, a process that occurs after crosslinking of a variety of signaling receptors and is thought to potentiate cellular activation. To investigate lipid raft dynamics during BCR signaling, we quantitatively analyzed the B cell lipid raft proteome. BCR engagement induced dissociation of the adaptor protein ezrin from lipid rafts as well as threonine dephosphorylation of ezrin and its concomitant detachment from actin, indicating a transient uncoupling of lipid rafts from the actin cytoskeleton. Expression of constitutively active ezrin chimeras inhibited the BCR-induced coalescence of lipid rafts. Our data demonstrate that the release of ezrin from lipid rafts acts as a critical trigger that regulates lipid raft dynamics during BCR signaling.
- Publication
Nature immunology, 2006, Vol 7, Issue 6, p625
- ISSN
1529-2908
- Publication type
Journal Article
- DOI
10.1038/ni1337