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Deretic N, Bolger-Munro M, Choi K, et al. The Actin-Disassembly Protein Glia Maturation Factor γ Enhances Actin Remodeling and B Cell Antigen Receptor Signaling at the Immune Synapse. Front Cell Dev Biol. 2021;9:647063doi: 10.3389/fcell.2021.647063.
Deretic, N., Bolger-Munro, M., Choi, K., Abraham, L., & Gold, M. R. (2021). The Actin-Disassembly Protein Glia Maturation Factor γ Enhances Actin Remodeling and B Cell Antigen Receptor Signaling at the Immune Synapse. Frontiers in cell and developmental biology, 9647063. https://doi.org/10.3389/fcell.2021.647063
Deretic, Nikola, et al. "The Actin-Disassembly Protein Glia Maturation Factor γ Enhances Actin Remodeling and B Cell Antigen Receptor Signaling at the Immune Synapse." Frontiers in cell and developmental biology vol. 9 (2021): 647063. doi: https://doi.org/10.3389/fcell.2021.647063
Deretic N, Bolger-Munro M, Choi K, Abraham L, Gold MR. The Actin-Disassembly Protein Glia Maturation Factor γ Enhances Actin Remodeling and B Cell Antigen Receptor Signaling at the Immune Synapse. Front Cell Dev Biol. 2021 Jul 09;9:647063. doi: 10.3389/fcell.2021.647063. eCollection 2021. PMID: 34336818; PMCID: PMC8318000.
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Front Cell Dev Biol. 2021 Jul 09;9:647063. doi: 10.3389/fcell.2021.647063. eCollection 2021.

The Actin-Disassembly Protein Glia Maturation Factor γ Enhances Actin Remodeling and B Cell Antigen Receptor Signaling at the Immune Synapse.

Frontiers in cell and developmental biology

Nikola Deretic, Madison Bolger-Munro, Kate Choi, Libin Abraham, Michael R Gold

Affiliations

  1. Department of Microbiology and Immunology, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada.

PMID: 34336818 PMCID: PMC8318000 DOI: 10.3389/fcell.2021.647063

Abstract

Signaling by the B cell antigen receptor (BCR) initiates actin remodeling. The assembly of branched actin networks that are nucleated by the Arp2/3 complex exert outward force on the plasma membrane, allowing B cells to form membrane protrusions that can scan the surface of antigen-presenting cells (APCs). The resulting Arp2/3 complex-dependent actin retrograde flow promotes the centripetal movement and progressive coalescence of BCR microclusters, which amplifies BCR signaling. Glia maturation factor γ (GMFγ) is an actin disassembly-protein that releases Arp2/3 complex-nucleated actin filaments from actin networks. By doing so, GMFγ could either oppose the actions of the Arp2/3 complex or support Arp2/3 complex-nucleated actin polymerization by contributing to the recycling of actin monomers and Arp2/3 complexes. We now show that reducing the levels of GMFγ in human B cell lines via transfection with a specific siRNA impairs the ability of B cells to spread on antigen-coated surfaces, decreases the velocity of actin retrograde flow, diminishes the coalescence of BCR microclusters into a central cluster at the B cell-APC contact site, and decreases APC-induced BCR signaling. These effects of depleting GMFγ are similar to what occurs when the Arp2/3 complex is inhibited. This suggests that GMFγ cooperates with the Arp2/3 complex to support BCR-induced actin remodeling and amplify BCR signaling at the immune synapse.

Copyright © 2021 Deretic, Bolger-Munro, Choi, Abraham and Gold.

Keywords: B cell; B cell receptor; actin; cell spreading; glia maturation factor-γ; immune synapse; signal transduction

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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