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Antigen-induced oligomerization of the B cell receptor is an early target of Fc gamma RIIB inhibition.

Liu, Wanli ; Won Sohn, Hae ; Tolar, Pavel ; Meckel, Tobias ; Pierce, Susan K. (2010)
Antigen-induced oligomerization of the B cell receptor is an early target of Fc gamma RIIB inhibition.
In: Journal of immunology (Baltimore, Md. : 1950), 184 (4)
Article, Bibliographie

Abstract

The FcgammaRIIB is a potent inhibitory coreceptor that blocks BCR signaling in response to immune complexes and, as such, plays a decisive role in regulating Ab responses. The recent application of high-resolution live cell imaging to B cell studies is providing new molecular details of the earliest events in the initiation BCR signaling that follow within seconds of Ag binding. In this study, we report that when colligated to the BCR through immune complexes, the FcgammaRIIB colocalizes with the BCR in microscopic clusters and blocks the earliest events that initiate BCR signaling, including the oligomerization of the BCR within these clusters, the active recruitment of BCRs to these clusters, and the resulting spreading and contraction response. Fluorescence resonance energy transfer analyses indicate that blocking these early events may not require molecular proximity of the cytoplasmic domains of the BCR and FcgammaRIIB, but relies on the rapid and sustained association of FcgammaRIIB with raft lipids in the membrane. These results may provide novel early targets for therapies aimed at regulating the FcgammaRIIB to control Ab responses in autoimmune disease.

Item Type: Article
Erschienen: 2010
Creators: Liu, Wanli ; Won Sohn, Hae ; Tolar, Pavel ; Meckel, Tobias ; Pierce, Susan K.
Type of entry: Bibliographie
Title: Antigen-induced oligomerization of the B cell receptor is an early target of Fc gamma RIIB inhibition.
Language: English
Date: 2010
Journal or Publication Title: Journal of immunology (Baltimore, Md. : 1950)
Volume of the journal: 184
Issue Number: 4
Abstract:

The FcgammaRIIB is a potent inhibitory coreceptor that blocks BCR signaling in response to immune complexes and, as such, plays a decisive role in regulating Ab responses. The recent application of high-resolution live cell imaging to B cell studies is providing new molecular details of the earliest events in the initiation BCR signaling that follow within seconds of Ag binding. In this study, we report that when colligated to the BCR through immune complexes, the FcgammaRIIB colocalizes with the BCR in microscopic clusters and blocks the earliest events that initiate BCR signaling, including the oligomerization of the BCR within these clusters, the active recruitment of BCRs to these clusters, and the resulting spreading and contraction response. Fluorescence resonance energy transfer analyses indicate that blocking these early events may not require molecular proximity of the cytoplasmic domains of the BCR and FcgammaRIIB, but relies on the rapid and sustained association of FcgammaRIIB with raft lipids in the membrane. These results may provide novel early targets for therapies aimed at regulating the FcgammaRIIB to control Ab responses in autoimmune disease.

Divisions: 10 Department of Biology
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10 Department of Biology > Plant Membrane Biophyscis (20.12.23 renamed in Biology of Algae and Protozoa)
10 Department of Biology > Membrane Dynamics
Date Deposited: 06 Jun 2011 13:12
Last Modified: 05 Mar 2013 09:48
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