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BENAROCH, P.

Publications and source records attributed to BENAROCH, P..

3 recordsLinked to original sources

GAS7 coordinates the activity of RAC1 and CDC42 to enhance macropinocytic surveillance and suppress motility in macrophages

Fluid uptake by macropinocytosis is central for the sentinel function of macrophages. However, how the actin network is organized at the cell surface to drive persistent membrane ruffling and macropinocytic cup formation remains unclear. Due to the high curvature of dorsal ruffles, we asked whether membrane curvature-associated proteins, such as those containing F-BAR domains, participate in this process. Here, leveraging public immune transcriptomic profiling and functional assays, we identify Growth Arrest Specific-7 (GAS7) as an F-BAR protein required for membrane ruffling and macropinocytosis in primary human monocyte-derived macrophages. GAS7 is enriched at dorsal ruffles and associates with actin regulators, sustaining high levels of active RAC1, to promote ruffle assembly. Moreover, GAS7 restrains the activation of CDC42, a GTPase linked to filopodia formation, cell motility and invasion. As a result, loss of GAS7 reduces ruffling and fluid uptake and instead promotes a phenotype characterized by increased motility, prominent filopodia, altered podosome dynamics, as well as an extracellular matrix-remodelling transcriptional program. Finally, we demonstrate that GAS7 enhances innate surveillance by augmenting the inflammatory response to muramyl dipeptide (NOD2 ligand) and by modulating the kinetics of TLR4 signalling to lipopolysaccharide. Thus, by coordinating RAC1 and CDC42 activities, GAS7 promotes macropinocytic uptake and enhances the macrophage responsiveness to microbial cues, while suppressing a more motile and invasive program.

cell biology↗

Single-cell RNA-Seq analysis reveals dual sensing of HIV-1 in blood Axl+ dendritic cells

Sensing of incoming viruses represents one of the pivotal tasks of dendritic cells (DC). Human primary blood DC encompass various subsets that are diverse in their susceptibility and response to HIV-1. The recent identification of Axl+DC, a new blood DC subset, endowed with unique capacities to bind, replicate, and transmit HIV-1 prompted us to evaluate its anti-viral response. We show that HIV-1 induced two main broad and intense transcriptional programs in different Axl+DC potentially induced by different sensors; a NF-{kappa}B-mediated program that led to DC maturation and efficient antigen-specific CD4+T cell activation, and a program mediated by STAT1/2 that activated type I IFN and an ISG response. These responses were absent from cDC2 exposed to HIV-1 except when viral replication occurred. Finally, Axl+DC actively replicating HIV-1 identified by quantification of viral transcripts exhibited a mixed NF-{kappa}B/ISG innate response. Our results suggest that the route of HIV-1 entry may dictate different innate sensing pathway by DC.

immunology↗

Release of HIV-1 particles from the viral compartment in macrophages requires an associated cytoskeleton and is driven by mechanical constraints

A defining feature of HIV-1 replication in macrophages is that viral assembly occurs at the limiting membrane of a compartment often named VCC (virus-containing compartments) that is connected to the extracellular medium. The newly formed viral progeny pinches of the membrane and accumulates in the lumen of the VCC. While HIV budding has been extensively studied, very little is known about how viral particles present in the lumen of VCC are released in the extracellular medium. Here we show that the actin dynamics are critical for this process by combining ultrastructural analyses, time-lapse microscopy and perturbations of the actin cytoskeleton. We found that jasplakinolide, which stabilizes actin fibres, inhibited viral release from HIV-1-infected macrophages. Furthermore, in jasplakinolide-treated macrophages, VCC became scattered and no longer co-localized with the integrin CD18, nor the phosphorylated form of the focal adhesion kinase PYK2. Inhibition of PYK2 activity in infected macrophages promoted intracellular retention of viral particles in VCC that were no longer connected to the plasma membrane. Finally, we stimulated the rapid release of viral particles from the VCC by subjecting infected macrophages to frustrated phagocytosis. As macrophages spread on IgG-coated glass surfaces, VCC rapidly migrated to the basal membrane and released their viral content in the extracellular medium, which required their association with CD18 and the actin cytoskeleton. These results highlight that VCC trafficking and virus release are intimately linked to the reorganization of the macrophage actin cytoskeleton in response to external physical cues, suggesting that it might be regulated in tissues by the mechanical stress to which these cells are exposed.

cell biology↗