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Antibodies
Special Issues
B Cell Antigen Receptor: Structure and Function
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B Cell Antigen Receptor: Structure and Function

A special issue of Antibodies (ISSN 2073-4468).

Deadline for manuscript submissions: closed (31 December 2017) | Viewed by 7065

Special Issue Editor

Prof. Dr. Anthony DeFranco

E-Mail Website
Guest Editor
Department of Microbiology and Immunology, University of California, San Francisco, CA 94143, USA
Interests: BCR signaling and function of TLRs

Special Issue Information

Dear Colleagues,

This Special Issue of Antibodies focuses on the structure and function of the B cell antigen receptor (BCR) and the pre-BCR. Authors will cover topics of current research related to receptor structure, receptor signaling, interactions with co-receptors, receptor expression and distribution on the cell surface, receptor internalization and functional consequences of receptor expression, signaling, and internalization of antigen. How BCR structure and signaling support the normal regulation of antibody production vs. dysregulated antibody production in autoimmune disease will also be considered.

Prof. Dr. Anthony DeFranco
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antibodies is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • BCR
  • Receptor signaling
  • B lymphocytes
  • Pre-BCR

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Published Papers (1 paper)

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Research

3166 KiB  
Article
Modulation of BCR Signaling by the Induced Dimerization of Receptor-Associated SYK
by Mark L. Westbroek and Robert L. Geahlen
Antibodies 2017, 6(4), 23; https://doi.org/10.3390/antib6040023 - 7 Dec 2017
Cited by 3 | Viewed by 6442
Abstract
Clustering of the B cell antigen receptor (BCR) by polyvalent antigens is transmitted through the SYK tyrosine kinase to the activation of multiple intracellular pathways that determine the physiological consequences of receptor engagement. To explore factors that modulate the quantity and quality of [...] Read more.
Clustering of the B cell antigen receptor (BCR) by polyvalent antigens is transmitted through the SYK tyrosine kinase to the activation of multiple intracellular pathways that determine the physiological consequences of receptor engagement. To explore factors that modulate the quantity and quality of signals sent by the crosslinked BCR, we developed a novel chemical mediator of dimerization to induce clustering of receptor-associated SYK. To accomplish this, we fused SYK with E. coli dihydrofolate reductase (eDHFR), which binds the small molecule trimethoprim (TMP) with high affinity and selectivity and synthesized a dimer of TMP with a flexible linker. The TMP dimer is able to induce the aggregation of eDHFR-linked SYK in live cells. The induced dimerization of SYK bound to the BCR differentially regulates the activation of downstream transcription factors, promoting the activation of Nuclear Factor of Activated T cells (NFAT) without affecting the activation of NFκB. The dimerization of SYK enhances the duration but not the amplitude of calcium mobilization by enhancing the extent and duration of its interaction with the crosslinked BCR at the plasma membrane. Full article
(This article belongs to the Special Issue B Cell Antigen Receptor: Structure and Function)
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