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Vamosi, G.

Publications and source records attributed to Vamosi, G..

2 recordsLinked to original sources

MHC Molecules on B Cell Microvilli Are Spatially Associated with IL-15Rα

Interleukin-15 (IL-15) trans-presentation (TP) by B cells is an important mechanism of T-cell activation; however, the spatial organisation of interleukin-15 receptor (IL-15R) relative to major histocompatibility complex (MHC) molecules on B-cell microvilli remains poorly understood. As microvilli protrude from the B-cell surface and may serve as sites of initial B cell-T-cell contact, the distribution of IL-15R and MHC molecules within these structures may be important during the earliest stages of T-cell recognition and activation. Here, we investigated the spatial association and molecular proximity of IL-15R with MHC class I and class II molecules on B-cell microvilli before immunological synapse formation, using confocal microscopy, stimulated emission depletion (STED) microscopy, stochastic optical reconstruction microscopy (STORM), and fluorescence lifetime imaging microscopy-based Forster resonance energy transfer (FLIM-FRET). Both MHC class I and class II molecules showed significant spatial association with IL-15R; however, the extent of colocalisation decreased as spatial resolution increased. STED microscopy revealed significant colocalisation between IL-15R and MHC class I, whereas STORM did not detect this association. In contrast, IL-15R and MHC class II remained significantly colocalised at both resolutions. FLIM-FRET further demonstrated molecular proximity between IL-15R and both MHC class I and class II molecules, with higher FRET efficiency observed for MHC class II. Collectively, these findings indicate that IL-15R is spatially organised in proximity to both MHC class I and class II molecules on B-cell microvilli before immunological synapse formation. This arrangement at potential sites of initial B-cell-T-cell contact may facilitate the coordination of IL-15 trans-presentation and antigen presentation during the earliest stages of B-cell-T-cell interactions.

cell biology↗

Soluble, but not precursor EGF induces intracrine signaling of the EGFR

EGFR is a transmembrane receptor tyrosine kinase regulating growth and survival in epithelial tissues. Its ligand, the epidermal growth factor (EGF), is produced as a membrane-anchored precursor (preEGF) that is proteolytically cleaved to release soluble EGF (sEGF). EGFR overexpression can convert it from a physiological regulator into an oncogenic driver. Therapeutic strategies targeting EGFR include monoclonal antibodies (mAbs) and tyrosine kinase inhibitors (TKIs). Although mAbs such as cetuximab initially block EGFR activity, tumors often develop resistance. Recent findings indicate that sEGF can activate EGFR within intracellular vesicles, promoting intracrine signaling that sustains proliferation despite extracellular inhibition. Here, we investigated the mechanism of intracrine EGFR signaling in the Golgi apparatus using confocal microscopy, FRET and fluorescence correlation spectroscopy. sEGF, but not preEGF, bound and induced EGFR dimerization and phosphorylation. Erlotinib, a membrane permeable TKI, effectively blocked phosphorylation, whereas extracellular cetuximab did not. These findings imply sEGF-induced intracrine EGFR signaling in the Golgi. Our results may shed light on a potential resistance mechanism to antibody treatment.

biophysics↗