TNFR1 mediates heterogeneity in single-cell NF-κB activation.

Nuclear factor kappa B (NF-κB) is a key regulator in immune signaling and is known to exhibit a digital activation pattern. Yet the molecular basis underlying the heterogeneity in NF-κB activation at single-cell level is not entirely understood. Here, we show that NF-κB activation in single cells is largely regulated by intrinsic differences at the receptor level.

Chip assisted formation of phase-separated liposomes for reconstituting spatial protein-lipid interactions.

Spatially organized molecular interactions are fundamental features underlying many biochemical processes in cells. These spatially defined reactions are essential to ensure high signaling specificity and are indispensable for maintaining cell functions. The construction of synthetic cell models that can resemble such properties is thus important yet less investigated.