Nature Immunology 7, 625 - 633 (2006)
Published online: 30 April 2006; | doi:10.1038/ni1337
Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor–mediated lipid raft dynamicsNeetu Gupta1, Bernd Wollscheid2, Julian D Watts2, Barbara Scheer1, Ruedi Aebersold2, 3
& Anthony L DeFranco11
Department of Microbiology and Immunology, University of California, San Francisco, California 94143, USA. 2
Institute for Systems Biology, Seattle, Washington 98103, USA. 3
Present address: Institute for Molecular Systems Biology, Swiss Federal Institute of Technology, CH-8093 Zurich, and Faculty of Natural Science, University of Zurich, CH-8057 Zurich, Switzerland.
Correspondence should be addressed to Anthony L DeFranco defranco@cgl.ucsf.edu 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.
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