Catálogo de publicaciones - revistas

<jats:title>Skin infection triggers fat responses</jats:title> <jats:p> Obesity is associated with chronic inflammation, but does fat tissue offer protection during infection? Zhang <jats:italic>et al.</jats:italic> noticed that the fat layers in the skin of mice thickened after inoculation with the pathogenic bacterium <jats:italic>Staphylococcus aureus</jats:italic> (see the Perspective by Alcorn and Kolls). Mutant mice incapable of forming new fat cells were more susceptible to infection. The differentiating fat cells secreted a small-molecule peptide called cathelicidin, specifically in response to the infection. By contrast, mature fat cells produce less cathelicidin, and are thus less protective. </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" issue="6217" page="67" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.1260972">67</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6217" page="26" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.aaa4567">26</jats:related-article> </jats:p>

<jats:title>Targeting EV-D68, a respiratory virus</jats:title> <jats:p> A recent outbreak of respiratory illness in U.S. children was caused by entorovirus D68 (EV-D68). Enteroviruses also include human pathogens such as human rhinovirus, which causes the common cold, and poliovirus. Most of these viruses are stabilized by a factor that binds in a hydrophobic pocket of the capsid protein VP1, and antiviral compounds can act by displacing this factor. Liu <jats:italic>et al.</jats:italic> report the crystal structure of EV-D68 and its complex with the antiviral compound peconaril. In EV-D68, the hydrophobic pocket contained a fatty acid that was displaced by peconaril. Peconaril efficiently inhibited EV-D68 infection of cells, making it a possible drug candidate against EV-D68. </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" issue="6217" page="71" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.1261962">71</jats:related-article> </jats:p>

<jats:title>Tagging truncated proteins with CAT tails</jats:title> <jats:p> During the translation of a messenger RNA (mRNA) into protein, ribosomes can sometimes stall. Truncated proteins thus formed can be toxic to the cell and must be destroyed. Shen <jats:italic>et al.</jats:italic> show that the proteins Ltn1p and Rqc2p, subunits of the ribosome quality control complex, bind to the stalled and partially disassembled ribosome. Ltn1p, a ubiquitin ligase, binds near the nascent polypeptide exit tunnel on the ribosome, well placed to tag the truncated protein for destruction. The Rqc2p protein interacts with the transfer RNA binding sites on the partial ribosome and recruits alanine- and threonine-bearing tRNAs. Rqc2p then catalyzes the addition of these amino acids onto the unfinished protein, in the absence of both the fully assembled ribosome and mRNA. These so-called CAT tails may promote the heat shock response, which helps buffer against malformed proteins. </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" issue="6217" page="75" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.1259724">75</jats:related-article> </jats:p>

<jats:title>Crunching the numbers to explain cancer</jats:title> <jats:p>Why do some tissues give rise to cancer in humans a million times more frequently than others? Tomasetti and Vogelstein conclude that these differences can be explained by the number of stem cell divisions. By plotting the lifetime incidence of various cancers against the estimated number of normal stem cell divisions in the corresponding tissues over a lifetime, they found a strong correlation extending over five orders of magnitude. This suggests that random errors occurring during DNA replication in normal stem cells are a major contributing factor in cancer development. Remarkably, this “bad luck” component explains a far greater number of cancers than do hereditary and environmental factors.</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" issue="6217" page="78" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.1260825">78</jats:related-article> </jats:p>

<jats:title>Men beware, when smoke gets in your Y's</jats:title> <jats:p> The relationship between tobacco smoking and elevated cancer risk has been recognized for 60 years. Yet what smoking does to our genetic material is still not fully understood. New work suggests that men should be particularly concerned. In a study of over 6000 men, Dumanski <jats:italic>et al.</jats:italic> find that men who smoke are more than three times as likely as nonsmokers to show loss of the Y chromosome in their blood cells. Whether this is a causal factor in cancer development or simply a marker of more consequential damage on other chromosomes could not be deduced from the study. </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" issue="6217" page="81" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.1262092">81</jats:related-article> </jats:p>

<jats:title>Lysosomes signal the nucleus to control aging</jats:title> <jats:p> Folick <jats:italic>et al.</jats:italic> propose a mechanism by which a lysosomal enzyme influences nuclear events that control longevity in the worm (see the Perspective by Shuo and Brunet). Increased expression of the lysosomal acid lipase LIPL-4 increased longevity, and this effect depended on the presence of the lysosomal lipid-binding protein LBP-8. LBP-8 acts as a chaperone that helps carry lipds to the nucleus. The authors identified the fatty acid oleoylethanolamide (OEA) as a potential signaling molecule whose transport to the nucleus could activate nuclear hormone receptors and transcription factors NHR-49 and NHR-80. The transcriptional targets of NHR-49 and NHR-80 in turn regulate longevity. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. 83 </jats:p>

<jats:p>On this week's show: Measuring the success of massive open online courses.</jats:p>

<jats:p>A weekly roundup of information on newly offered instrumentation, apparatus, and laboratory materials of potential interest to researchers.</jats:p>