Catálogo de publicaciones - revistas

<jats:title>Liquid droplets step on the cGAS</jats:title> <jats:p>Spontaneous partitioning of a homogeneous solution of molecules, or liquid-phase separation, underlies the formation of cellular bodies from P granules to nucleoli. Essentially, dense-phase liquid droplets act like cellular compartments. Du and Chen show that DNA binding to its cytoplasmic sensor, cyclic GMP–AMP synthase (cGAS), results in liquid droplets containing activated cGAS (see the Perspective by Ablasser). This phenomenon occurs through multivalent interactions, augmented by zinc, between DNA binding domains on cGAS and DNA in a length-dependent manner. Binding triggers a switchlike reaction that concentrates the enzyme and reactants to enhance STING-dependent interferon responses.</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="6403" page="704" related-article-type="in-this-issue" vol="361" xlink:href="10.1126/science.aat1022">704</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6403" page="646" related-article-type="in-this-issue" vol="361" xlink:href="10.1126/science.aau6019">646</jats:related-article> </jats:p>

<jats:title>Fragile X and fragile translation in flies</jats:title> <jats:p> Mutations in the fragile X mental retardation 1 ( <jats:italic>FMR1</jats:italic> ) gene underlie fragile X syndrome and fragile X–associated primary ovarian insufficiency, which are prominent intellectual disability and reproductive disorders, respectively. FMR1 is thought to reduce protein synthesis (translation) at synapses. In <jats:italic>Drosophila</jats:italic> oocytes, Greenblatt and Spradling found that <jats:italic>Fmr1</jats:italic> loss leads to oocytes that generate embryos exhibiting neural defects (see the Perspective by Aryal and Klann). Ribosome profiling of oocytes identified a specific role for FMR1 in enhancing the translation of large proteins, including many associated with autism. FMR1 seems to help maintain translation of large mRNAs that otherwise condense into inactive ribonucleoprotein particles. This mechanism may underlie other causes of autism and mental dysfunction. </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="6403" page="709" related-article-type="in-this-issue" vol="361" xlink:href="10.1126/science.aas9963">709</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6403" page="648" related-article-type="in-this-issue" vol="361" xlink:href="10.1126/science.aau6450">648</jats:related-article> </jats:p>

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