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Shen et al. found that calibrated CAR signaling promotes asymmetric cell division (ACD) by enhancing the microtubule-organizing center (MTOC)-CAR immune synapse (CARIS) coupling through localized PLCγ1-DAG signaling. This signaling-associated asymmetry contributes to the generation of memory-like CAR-T cell progeny and is linked to improved persistence and antitumor efficacy in vivo.

YouTube video by Mary Trump Media

YouTube video by Mary Trump Media

YouTube video by Mary Trump Media

YouTube video by Mary Trump Media

YouTube video by Mary Trump Media

YouTube video by Mary Trump Media

The NLRP3 inflammasome contributes to a wide range of conditions from infections to Alzheimer’s disease. NLRP3 forms an inactive decameric cage, that upon interaction with the trans-Golgi network (TGN) and microtubule organization center (MTOC), leads to inflammasome activation, yet whether non-decamer NLRP3 species form functional inflammasomes remains unclear. Here, we design a NLRP3 exon 3 deletion variant that forms low molecular weight NLRP3 assemblies. Spatially and dynamically highly resolved microscopy in THP-1 and human macrophages shows that nigericin, a K+-dependent NLRP3 stimulus, can trigger two distinct activation pathways: (i) the rapidly engaged decameric cage-dependent pathway; and (ii) a decameric cage-independent, TGN/MTOC-distal, and slow-reacting pathway employed by low molecular weight NLRP3 species, that dominates in human neutrophils. Collectively, our results delineate two parallel yet biologically distinct NLRP3 activation pathways, thereby providing

NLRP3 normally forms a decamer to interact with trans-Golgi network (TGN) and microtubule organization center (MTOC) for inflammasome activation. Here the authors generate an exon 3-deficient NLRP3 to show that the resulting non-decameric, smaller NLRP3 forms a TGN/MTOC-distal complex that responds to nigericin and dominates in human neutrophils.

NLRP3 normally forms a decamer to interact with trans-Golgi network (TGN) and microtubule organization center (MTOC) for inflammasome activation. Here the authors generate an exon 3-deficient NLRP3 to...

NLRP3 normally forms a decamer to interact with trans-Golgi network (TGN) and microtubule organization center (MTOC) for inflammasome activation. Here the authors generate an exon 3-deficient NLRP3 to show that the resulting non-decameric, smaller NLRP3 forms a TGN/MTOC-distal complex that responds to nigericin and dominates in human neutrophils.

NLRP3 normally forms a decamer to interact with trans-Golgi network (TGN) and microtubule organization center (MTOC) for inflammasome activation. Here the authors generate an exon 3-deficient NLRP3 to show that the resulting non-decameric, smaller NLRP3 forms a TGN/MTOC-distal complex that responds to nigericin and dominates in human neutrophils.