2. Academic Validation
  3. B cell receptor-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

  • J Cell Sci. 2023 Jul 7;jcs.261119. doi: 10.1242/jcs.261119.
Luqman O Awoniyi 1 2 3,  Diogo M Cunha 1 2 3,  Alexey V Sarapulov 1 2 3,  Sara Hernández-Pérez 1 2 3,  Marika Runsala 1 2 3,  Blanca Tejeda-González 1 2 3,  Vid Šuštar 1,  M Özge Balci 1 2 3,  Petar Petrov 1 2 3,  Pieta K Mattila 1 2 3
Affiliations

Affiliations

  • 1 Institute of Biomedicine and MediCity Research Laboratories, University of Turku, Turku, Finland.
  • 2 Turku Bioscience, University of Turku and Åbo Akademi University, Turku, Finland.
  • 3 InFLAMES Research Flagship Center, University of Turku, Finland.
PMID: 37417469 DOI: 10.1242/jcs.261119
Abstract

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.

Keywords

APEX2; B cells; BCR; Lipid rafts; Proximity proteomics; Receptor signalling.

Figures
Products