The SNARE protein Vti1b is recruited to the sites of BCR activation but is redundant for antigen internalisation, processing and presentation

Music, Amna; Tejeda-González, Blanca; Cunha, Diogo M; Mollard, Gabriele Fischer von; Hernández-Pérez, Sara; Mattila, Pieta K.

doi:10.3389/fcell.2022.987148

Cited by 4 publications

(3 citation statements)

References 38 publications

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“…5). We characterized its endomembrane localization in B cells and showed its enrichment to the sites of BCR signaling, further supporting the potential of our dataset, although we could not demonstrate a functional role for Vti1b in B cell activation ( Music et al ., 2022). Interestingly, our dataset revealed various proteins linked to SUMOylation pathways.…”

Section: Discussionsupporting

confidence: 77%

BCR-induced protein dynamics and the emerging role of SUMOylation revealed by proximity proteomics

Awoniyi

Runsala

Šuštar

et al. 2020

Preprint

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B lymphocytes form a central part of the adaptive immune system, helping to clear infections by mounting antibody responses and immunological memory. B cell activation is critically controlled by a specific antigen receptor, the B cell receptor (BCR), which triggers a complex, multibranched signaling cascade initiating various cellular changes. While parts of these pathways are reasonably well characterized, we still lack a comprehensive protein-level view of the very dynamic and robust cellular response triggered by antigen engagement. Ability to track, with sufficient kinetic resolution, the protein machineries responding to BCR signaling is imperative to provide new understanding into this complex cell activation event. We address this challenge by using APEX2 proximity labeling technique, that allows capture a major fraction of proteins in a given location with 20nm range and 1min time window, and target the APEX2 enzyme to the plasma membrane lipid raft domain, where BCR efficiently translocates upon activation. Our data provides unprecedented insights into the protein composition of lipid raft environment in B cells, and the changes triggered there upon BCR cross-linking and translocation. In total, we identified 1677 proteins locating at the vicinity of lipid raft domains in cultured mouse B cells. The data includes a majority of proteins known to be involved in proximal BCR signaling. Interestingly, our differential enrichment analysis identified various proteins that underwent dynamic changes in their localization but that had no previously known linkage to early B cell activation. As expected, we also identified, for example, a wealth of proteins linked to clathrin-mediated endocytosis that were recruited to the lipid rafts upon cell activation. We believe that his data serves as a valuable record of proteins involved in BCR activation response and aid various future studies in the field.

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Section: Discussionsupporting

confidence: 77%

BCR-induced protein dynamics and the emerging role of SUMOylation revealed by proximity proteomics

Awoniyi

Runsala

Šuštar

et al. 2020

Preprint

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“…5 A). We characterized its enrichment to the sites of BCR signaling, further supporting the potential of our dataset ( Music et al, 2022 ).…”

Section: Discussionsupporting

confidence: 68%

B cell receptor-induced protein dynamics and the emerging role of SUMOylation revealed by proximity proteomics

Awoniyi

Cunha

Sarapulov

et al. 2023

Journal of Cell Science

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Successful B cell activation, critical for high-affinity antibody production, is controlled by the B cell antigen receptor (BCR). However, we still lack a comprehensive protein-level view of the very dynamic multi-branched cellular events triggered by antigen binding. Here, we employed APEX2 proximity biotinylation to study antigen-induced changes, 5-15 min after receptor activation, at the vicinity of the plasma membrane lipid rafts, wherein BCR enriches upon activation. The data reveals dynamics of signaling proteins, as well as various players linked to the subsequent processes, such as actin cytoskeleton remodelling and endocytosis. Interestingly, our differential expression analysis identified dynamic responses in various proteins previously not linked to early B cell activation. We demonstrate active SUMOylation at the sites of BCR activation in various conditions and report its functional role in BCR signaling through Akt and MAPK axes.

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“…As the function of immune cells is to be sensitized by pathogenic products, it is not surprising that upon exposure, lysosomes are remodeled in different ways. Various vesicle-linked proteins have been shown to alter their intracellular positioning, for instance, upon BCR engagement (Music et al, 2022;Awoniyi et al, 2023). However, more efforts are required to dissect the functions of the different endosomal players in B cell activation.…”

Section: Hämälistö Et Almentioning

confidence: 99%

Endolysosomal vesicles at the center of B cell activation

Hämälistö,

Del Valle Batalla,

Yuseff

et al. 2024

Journal of Cell Biology

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The endolysosomal system specializes in degrading cellular components and is crucial to maintaining homeostasis and adapting rapidly to metabolic and environmental cues. Cells of the immune system exploit this network to process antigens or promote cell death by secreting lysosome-related vesicles. In B lymphocytes, lysosomes are harnessed to facilitate the extraction of antigens and to promote their processing into peptides for presentation to T cells, critical steps to mount protective high-affinity antibody responses. Intriguingly, lysosomal vesicles are now considered important signaling units within cells and also display secretory functions by releasing their content to the extracellular space. In this review, we focus on how B cells use pathways involved in the intracellular trafficking, secretion, and function of endolysosomes to promote adaptive immune responses. A basic understanding of such mechanisms poses an interesting frontier for the development of therapeutic strategies in the context of cancer and autoimmune diseases.

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The SNARE protein Vti1b is recruited to the sites of BCR activation but is redundant for antigen internalisation, processing and presentation

Cited by 4 publications

References 38 publications

BCR-induced protein dynamics and the emerging role of SUMOylation revealed by proximity proteomics

BCR-induced protein dynamics and the emerging role of SUMOylation revealed by proximity proteomics

B cell receptor-induced protein dynamics and the emerging role of SUMOylation revealed by proximity proteomics

Endolysosomal vesicles at the center of B cell activation

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