Mapping the nanoscale organization of the human cell surface proteome reveals new functional associations and surface antigen clusters.

ABSTRACT: The cell surface is a dynamic interface that controls cell-cell communication and signal transduction relevant to organ development, homeostasis and repair, immune reactivity, and pathologies driven by aberrant cell surface phenotypes. The spatial organization of cell surface proteins is central to these processes. High-resolution fluorescence microscopy and proximity labeling have advanced studies of surface protein associations, but the spatial organization of the complete surface proteome remains uncharted. In this study, we systematically mapped the surface proteome of human T-lymphocytes and B-lymphoblasts using proximity labeling of 85 antigens, identified from over 100 antibodies tested for binding to surface-exposed proteins. These experiments were coupled with an optimized data-in

SUBMITTER: Floyd BM 

PROVIDER: S-EPMC11870420 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature