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

Luqman O. Awoniyi, Diogo M. Cunha, Alexey V. Sarapulov, Sara Hernández-Pérez, Marika Runsala, Blanca Tejeda-González, Vid Šuštar, M. Özge Balci, Petar Petrov, Pieta K. Mattila*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

2 Citations (Scopus)
13 Downloads (Pure)

Abstract

Successful B cell activation, which is 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 remodeling 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 the AKT and ERK1/2 axes.

Original languageEnglish
Article numberjcs261119
Number of pages18
JournalJournal of Cell Science
Volume136
Issue number15
DOIs
Publication statusPublished - Aug 2023
MoE publication typeA1 Journal article-refereed

Keywords

  • APEX2
  • B cells
  • BCR signaling
  • Golga3
  • Lipid rafts
  • SUMOylation

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