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Eutectogels are emerging as an appealing soft conductor for self‐powered sensing and the next generation of flexible human–computer interactive devices owing to their inherent mechanical elasticity and high ionic conductivity. However, it still remains a challenge to simultaneously achieve multi‐functional and multi‐response integrations through a facile and sustainable approach. Herein, a self‐healing, environment tolerant, intrinsically conductive, and recyclable eutectogel with multiple responses is developed via one‐step solar‐initiated polymerization of deep eutectic solvents (DESs) and ionic liquids (ILs). Abundant hydrogen bonds and ion‐dipole interactions impart eutectogels with high mechanical strength (8.8 MPa), ultra‐stretchability (>1100%), strong self‐adhesion (≈12 MPa), recyclability, and autonomously self‐healing ability. Furthermore, the intrinsically conductive eutectogels with appealing versatile sensations on strain, temperature, and humidity can serve as wearable sensors for wireless motion recognition and human–computer interaction control. More importantly, the eutectogel‐assembled single‐electrode triboelectric nanogenerator (TENG) exhibits extreme environment‐tolerant and fast self‐healable properties that contribute to maintaining excellent and stable electrical outputs in a wide work temperature range (approximately −40–60 °C), which appear to be promising in self‐powered flexible electronics with high environmental adaptability. [ABSTRACT FROM AUTHOR]

eIF3, whose subunits are frequently overexpressed in cancer, regulates mRNA translation from initiation to termination, but mRNA‐selective functions of individual subunits remain poorly defined. Using multiomic profiling upon acute depletion of eIF3 subunits, we observed that while eIF3a, b, e, and f markedly differed in their impact on eIF3 holo‐complex formation and translation, they were each required for cancer cell proliferation and tumor growth. Remarkably, eIF3k showed the opposite pattern with depletion promoting global translation, cell proliferation, tumor growth, and stress resistance through repressing the synthesis of ribosomal proteins, especially RPS15A. Whereas ectopic expression of RPS15A mimicked the anabolic effects of eIF3k depletion, disruption of eIF3 binding to the 5′‐UTR of RSP15A mRNA negated them. eIF3k and eIF3l are selectively downregulated in response to endoplasmic reticulum and oxidative stress. Supported by mathematical modeling, our data uncover eIF3k‐l as a mRNA‐specific module which, through controlling RPS15A translation, serves as a rheostat of ribosome content, possibly to secure spare translational capacity that can be mobilized during stress. Are there mRNA‐selective functions of individual eIF3 subunits? Here, multiomic profiling upon acute depletion of eIF3 subunits uncovers eIF3k‐l as an mRNA‐specific module that serves as a rheostat of ribosome content, securing spare translational capacity that can be mobilized during stress. Acute depletion of eIF3 subunits has subunit‐selective impact on holo‐eIF3 architecture.eIF3k depletion uniquely causes increased tumor growth and ribosome content.eIF3k depletion boosts the translation of RPS15A mRNA through an eIF3‐binding site in the 5′‐UTR.eIF3k and eIF3l are selectively downregulated by cellular stress, thus promoting cell survival. [ABSTRACT FROM AUTHOR]

Exposure to heat stress triggers a well‐defined acute response marked by HSF1‐dependent transcriptional upregulation of heat shock proteins. Cells allowed to recover acquire thermotolerance, but this adaptation is poorly understood. By quantitative proteomics, we discovered selective upregulation of HSP70‐family chaperone HSPA1 and its co‐factors, HSPH1 and DNAJB1, in MCF7 breast cancer cells acquiring thermotolerance. HSPA1 was found to have dual function during heat stress response: (i) During acute stress, it promotes the recruitment of the 26S proteasome to translating ribosomes, thus poising cells for rapid protein degradation and resumption of protein synthesis upon recovery; (ii) during thermotolerance, HSPA1 together with HSPH1 maintains ubiquitylated nascent/newly synthesized proteins in a soluble state required for their efficient proteasomal clearance. Consistently, deletion of HSPH1 impedes thermotolerance and esophageal tumor growth in mice, thus providing a potential explanation for the poor prognosis of digestive tract cancers with high HSPH1 and nominating HSPH1 as a cancer drug target. We propose dual roles of HSPA1 either alone or in complex with HSPH1 and DNAJB1 in promoting quality control of nascent/newly synthesized proteins and cellular thermotolerance. Synopsis: How cells exposed to heat stress acquire thermotolerance is poorly understood. Here, quantitative proteomics identifies upregulation of HSP70‐family chaperone HSPA1, which fulfills dual function in quality control of nascent proteins at translating ribosomes. Proteotoxic stress causes translation arrest, ubiquitylation of nascent/newly synthesized proteins, and proteasome recruitment to ribosomes.Proteasome recruitment to ribosomes is augmented by HSP70 activity independently of nascent chain ubiquitylation.HSPA1 in complex with HSPH1‐DNAJB1 cofactors maintains solubility and proteasomal clearance of ubiquitylated proteins.Low HSPH1 expression impedes nascent‐protein quality control and tumor growth, correlating with favorable outcome. [ABSTRACT FROM AUTHOR]

The tetraspan protein KAI1 ( CD82) has been previously shown to have important roles in cell migration, invasion, and melanoma prognosis. In this study, we investigated the role of KAI1 regarding melanoma angiogenesis. KAI1 overexpression strongly suppressed the growth of the human umbilical vein endothelial cells and their tubular structure formation in vitro. Also, KAI1 was able to inhibit both interleukin-6 ( IL-6) and VEGF at mRNA and protein levels. Using nude mice in the in vivo study, we showed that KAI1, through the regulation of ING4, inhibited blood vessel formation in matrigel plugs along with the downregulation of IL-6 and VEGF, and the recruitment of CD31-positive cells. Finally, we found that KAI1 was able to suppress the activity of a serine/threonine kinase Akt by suppressing Akt phosphorylation (Ser473). Taken together, our results suggested that KAI1 was able to suppress melanoma angiogenesis by downregulating IL-6 and VEGF expression, and the restoration of KAI1 functionality offered a new approach in human melanoma treatment. [ABSTRACT FROM AUTHOR]