Inflammasomes integrate cytosolic evidence of infection or damage to mount inflammatory responses. The inflammasome sensor NLRP1 is expressed in human keratinocytes and coordinates inflammation in the skin. We found that diverse stress signals induce human NLRP1 inflammasome assembly by activating MAP kinase p38: While the ribotoxic stress response to UV and microbial molecules exclusively activates p38 through MAP3K ZAKα, infection with arthropod-borne alphaviruses, including Semliki Forest and Chikungunya virus, activates p38 through ZAKα and potentially other MAP3K. We demonstrate that p38 directly phosphorylates NLRP1 and that serine 107 in the linker region is critical for activation. NLRP1 phosphorylation is followed by ubiquitination of NLRP1PYD, N-terminal degradation of NLRP1, and nucleation of inflammasomes by NLRP1UPA-CARD. In contrast, activation of NLRP1 by nanobody-mediated ubiquitination, viral proteases, or inhibition of DPP9 was independent of p38 activity. Taken together, we define p38 activation as a unifying signaling hub that controls NLRP1 inflammasome activation by integrating a variety of cellular stress signals relevant to the skin.

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This work aimed to study the removal of malachite green dye from wastewaters through adsorption using raw corn straw (RCS) and ultrasound-assisted modified corn straw (MCS). RCS and MCS were prepared and characterized in detail. The characterization indicated that RCS and MCS presented favorable structures for malachite green adsorption and that the ultrasound treatment provided a disorganization of the adsorbent's crystalline regions and also caused the formation of cavities and protuberances. The adsorption study was performed by equilibrium isotherms, kinetic curves, thermodynamic parameters, and application in real effluents composed of dye mixtures and inorganic compounds. The Elovich model was suitable for the adsorption kinetics and the Freundlich model was appropriate to represent the equilibrium. The maximum experimental adsorption capacities were 200 mg g for RCS and 210 mg g for MCS, obtained at 328 K. MCS was more effective than RCS to treat real effluents, attaining around 92% of color removal.

In this research, chitin and rice husks were used as adsorbents to recover cobalt from leached solutions of lithium-ion batteries. The waste materials were obtained and characterized. At first, the adsorption study was performed in batch systems using synthetic solutions, where the pH effect, kinetic, equilibrium, and thermodynamic aspects were investigated. Later, in the best conditions, chitin and rice husks were applied to recover cobalt from real leached solutions of lithium-ion batteries. For both materials, the adsorption was favoured at pH ¼ 6.0. The maximum adsorption capacities were 50.0 mg g À1 and 17.6 mg g À1 for chitin and rice husks, respectively, obtained at 318 K. The Co þ2 recovery percentages from real leached solutions were 95.0 % and 40.0 % for chitin and rice husks respectively. These results revealed that chitin can be used as an alternative and low-cost waste material to recover Co þ2 from real leached solutions of lithium-ion batteries.

Inflammasomes integrate cytosolic evidence of infection or damage to mount inflammatory responses. The inflammasome sensor NLRP1 is expressed in human keratinocytes and coordinates inflammation in the skin. We found that diverse stress signals converge on the activation of p38 kinases to initiate human NLRP1 inflammasome assembly: UV irradiation and microbial molecules that initiate the ribotoxic stress response critically relied on the MAP3 kinase ZAKα to activate p38 and ultimately human NLRP1. Infection with insect-transmitted alphaviruses, including Semliki Forest, Ross River, and Chikungunya virus, also activated NLRP1 in a p38-dependent manner. In the absence on ZAKα, inflammasome assembly was maintained, although at reduced levels, indicating contribution of other upstream kinases. NLRP1 activation by direct nanobody-mediated ubiquitination was independent of p38 activity. Stimulation of p38 by overexpression of MAP2 kinases MKK3 or MKK6 is sufficient for NLRP1 activation, and NLRP1 is directly phosphorylated by p38. Taken together, we define p38 activation as a unifying signaling hub that controls NLRP1 inflammasome activation by integrating a variety of cellular stress signals relevant to the skin.