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

Liu, Wanli and Won Sohn, Hae and Tolar, Pavel and Meckel, Tobias and 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), pp. 1977-89. ISSN 1550-6606,
[Article]

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 and Won Sohn, Hae and Tolar, Pavel and Meckel, Tobias and Pierce, Susan K.
Title: Antigen-induced oligomerization of the B cell receptor is an early target of Fc gamma RIIB inhibition.
Language: English
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.

Journal or Publication Title: Journal of immunology (Baltimore, Md. : 1950)
Journal volume: 184
Number: 4
Divisions: 10 Department of Biology
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10 Department of Biology > Plant Membrane Biophysics
10 Department of Biology > Membrane Dynamics
Date Deposited: 06 Jun 2011 13:12
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