Catálogo de publicaciones - revistas

<jats:title>Protecting the heart</jats:title> <jats:p> Excitation-contraction (E-C) coupling is fundamental to heart contraction. Junctophilin-2 is a structural protein required for formation of the E-C coupling machinery. During heart disease, stress-activated calpain cleaves junctophilin-2, disrupting the E-C coupling machinery and calcium ion signaling, which compromises cell contraction. Guo <jats:italic>et al.</jats:italic> found that under stress conditions, calpain-mediated cleavage converted full-length junctophilin-2 from a structural protein into a transcriptional regulator that shuttled to the nucleus (see the Perspective by Padmanabhan and Haldar). Furthermore, failing cardiomyocytes in stressed myocardium transduced mechanical information (E-C uncoupling) into transcriptional reprogramming. </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.aan3303">eaan3303</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6421" page="1359" related-article-type="in-this-issue" vol="362" xlink:href="10.1126/science.aav8956">1359</jats:related-article> </jats:p>

<jats:title>Cobalt unfettered by its ligand field</jats:title> <jats:p> Applied magnetic fields induce a field in any compound with unpaired electrons. However, for the induced field to persist once the applied field is gone, the electrons must be configured to manifest orbital angular momentum. Generally, the influence of ligands severely restricts that property in transition metal complexes. Bunting <jats:italic>et al.</jats:italic> now show that a cobalt ion is just barely affected by two linearly coordinated carbon ligands and, as such, exhibits maximal orbital angular momentum. Although its magnetic properties mainly pertain at very low temperature, its structure offers a more general design principle. </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.aat7319">eaat7319</jats:related-article> </jats:p>

<jats:title>Architecture of the human TRPM2 channel</jats:title> <jats:p> Adenosine diphosphate–ribose (ADPR) mediates calcium (Ca <jats:sup>2+</jats:sup> ) release by activating the transient receptor potential melastatin 2 (TRPM2) channel. Three structures now elucidate the conformational regulation mechanism of TRPM2 gating. Wang <jats:italic>et al.</jats:italic> describe cryo–electron microscopy structures of human TRPM2 in the apo, ADPR-bound, and ADPR- and Ca <jats:sup>2+</jats:sup> -bound states. In the apo state, both intra- and intersubunit interactions appeared to lock TRPM2 into a closed and autoinhibited state. ADPR binding disrupted some interactions and dramatically altered the TRPM2 conformation. Binding of Ca <jats:sup>2+</jats:sup> further primed the opening of the channel. </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.aav4809">eaav4809</jats:related-article> </jats:p>

<jats:title>Mechanism of promoter recognition</jats:title> <jats:p> To start transcription, RNA polymerase II is recruited by the general transcription factor IID (TFIID) to the DNA promoter. Patel <jats:italic>et al.</jats:italic> used a combination of experimental approaches to elucidate the full molecular architecture of human TFIID and its complete conformational landscape during promoter recognition. They suggest exactly how TFIID is loaded onto the promoter, which involves defined steps—including promoter recognition and transcription initiation—and leads to regulated gene expression. </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.aau8872">eaau8872</jats:related-article> </jats:p>