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Biology subjects

Psoma, A.

Publications and source records attributed to Psoma, A..

2 recordsLinked to original sources

T cells compete via reverse MHC class I signaling at the synapse with dendritic cells to secure Golgi recruitment for activation

Interleukin-12 (IL-12) is a key immunostimulatory cytokine produced by dendritic cells (DCs) upon infection that plays a central role in the activation and differentiation of cytotoxic T cells. Notably, IL-12 is secreted in a highly polarized manner from late endosomes or lysosomes at the contact interface between a DC and a T cell, known as the immunological synapse. However, the signaling mechanisms initiating this spatially restricted cytokine release remain poorly defined. Here, using artificial T cell mimics, beads coated with T cell surface ligands, we show that antigen recognition induces recruitment of the DCs microtubule organizing center (MTOC) and Golgi apparatus to the immunological synapse via reverse MHC class I signaling. Our results further indicate that the signaling pathways governing MTOC polarization are highly conserved in DCs, consistent with mechanisms described in other immune cell types. As newly synthesized IL-12 traffics through the Golgi, this intracellular reorientation facilitates localized release of IL-12 directly at the site of T cell engagement, likely enabling DCs to focus their stimulatory capacity on responsive T cells within the crowded environment of secondary lymphoid organs. Furthermore, by applying spatially patterned antibody arrays targeting MHC class I, we reveal that MTOC polarization is biased toward sites exhibiting the strongest reverse MHC class I signaling. This suggests that IL-12 is preferentially released at synapses formed with T cells displaying higher T cell receptor affinity, providing a mechanism for selection of the most potent T cell.

immunology↗

Butyrate blocks specific histone acetylation by preventing recruitment of p300 to acetylated histones

Butyrate, a short-chain fatty acid (SCFA) produced by microbial fermentation of dietary fiber, exerts beneficial metabolic and immunomodulatory functions through hyperactivation of the histone acetylase (HAT) p300 and inhibition of histone deacetylases (HDAC). These effects are widely believed to result in the acetylation of distinct histones that regulate specific genes, including at transcription starting sites (TSS) and enhancers. However, we show that this is not the case, as butyrate dose-dependently increases the acetylation of histones throughout the entire genome. Molecular dynamics simulations suggest that the RING-loop prevents the recruitment of p300 to acetylated histones through its bromodomain, and thereby cannot maintain the acetylation of specific histones through positive feedback. This was confirmed by showing that only catalytically inactive p300 stably binds to acetylated histones. Thus, the epigenetic regulation of specific genes by butyrate is limited, but butyrate instead increases histone acetylation globally resulting in opening of the entire chromatin structure.

molecular biology↗