Catálogo de publicaciones - revistas

<jats:title>Linking protein misfolding and innate immunity</jats:title> <jats:p> Multiple innate immune sensors undergo rapid assembly into large complexes known as signalosomes. This is an essential step during cellular responses to microbes and danger signals. How this process is regulated to avoid accumulation of potentially toxic protein aggregates remains poorly understood. Abdel-Nour <jats:italic>et al.</jats:italic> identified a pathway, dependent on heme-regulated inhibitor, eukaryotic initiation factor 2α, activating transcription factor 4, and heat shock protein B8, which controls the folding and scaffolding of innate immune sensors, allowing optimal proinflammatory signaling (see the Perspective by Pierre). The pathway appears to mirror the endoplasmic reticulum unfolded protein response (UPR), and so was named the cytosolic UPR (cUPR). The cUPR may represent a general mechanism to control protein misfolding in cells. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.aaw4144">eaaw4144</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6448" page="28" related-article-type="in-this-issue" vol="365" xlink:href="10.1126/science.aay0987">28</jats:related-article> </jats:p>

<jats:title>A metasurface polarization camera</jats:title> <jats:p> Imaging the polarization of light scattered from an object provides an additional degree of freedom for gaining information from a scene. Conventional polarimeters can be bulky and usually consist of mechanically moving parts (with a polarizer and analyzer setup rotating to reveal the degree of polarization). Rubin <jats:italic>et al.</jats:italic> designed a metasurface-based full-Stokes compact polarization camera without conventional polarization optics and without moving parts. The results provide a simplified route for polarization imaging. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.aax1839">eaax1839</jats:related-article> </jats:p>

<jats:title>Glycine N-degron regulation revealed</jats:title> <jats:p> For more than 30 years, N-terminal sequences have been known to influence protein stability, but additional features of these N-end rule, or N-degron, pathways continue to be uncovered. Timms <jats:italic>et al.</jats:italic> used a global protein stability (GPS) technology to take a broader look at these pathways in human cells. Unexpectedly, glycine exposed at the N terminus could act as a potent degron; proteins bearing N-terminal glycine were targeted for proteasomal degradation by two Cullin-RING E3 ubiquitin ligases through the substrate adaptors ZYG11B and ZER1. This pathway may be important, for example, to degrade proteins that fail to localize properly to cellular membranes and to destroy protein fragments generated during cell death. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.aaw4912">eaaw4912</jats:related-article> </jats:p>