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<jats:title>Signal Scaffolds</jats:title> <jats:p> Scaffolds in cellular signaling pathways are turning out to do way more than just hold proteins together in a complex. <jats:bold> Kim <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="867" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1232389">867</jats:related-article> , published online 11 April) showed the importance of the scaffold protein Axin as an active participant controlling the kinetics of activation of signaling through the pathways. Axin is part of two protein complexes that have opposing actions that may regulate the timing of signaling—either activating Wnt signaling, thus protecting β-catenin from destruction, or causing proteolytic destruction of β-catenin. <jats:bold> Rock <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="871" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1235822">871</jats:related-article> , published online 11 April) characterized the role of the scaffold protein Nud1 in the mitotic exit network and found that the kinase that produces the output from the signaling complex only interacts with a scaffold that is primed by its activator protein kinase, already bound to the scaffold and creating a docking site. </jats:p>

<jats:title>Signal Scaffolds</jats:title> <jats:p> Scaffolds in cellular signaling pathways are turning out to do way more than just hold proteins together in a complex. <jats:bold> Kim <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="867" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1232389">867</jats:related-article> , published online 11 April) showed the importance of the scaffold protein Axin as an active participant controlling the kinetics of activation of signaling through the pathways. Axin is part of two protein complexes that have opposing actions that may regulate the timing of signaling—either activating Wnt signaling, thus protecting β-catenin from destruction, or causing proteolytic destruction of β-catenin. <jats:bold> Rock <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="871" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1235822">871</jats:related-article> , published online 11 April) characterized the role of the scaffold protein Nud1 in the mitotic exit network and found that the kinase that produces the output from the signaling complex only interacts with a scaffold that is primed by its activator protein kinase, already bound to the scaffold and creating a docking site. </jats:p>

<jats:title>ATAXIN Clock</jats:title> <jats:p> Although core components of circadian clocks in flies and mammals are transcriptional circuits, recent evidence indicates posttranscriptional regulation of the clock occurs. Studies from <jats:bold>Lim and Allada</jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="875" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1234785">875</jats:related-article> ) and <jats:bold> Zhang <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="879" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1234746">879</jats:related-article> ) converge to show that the protein ATAXIN-2, associated with neurodegenerative diseases in humans, is a regulator of translation required for normal clock function in pacemaker neurons and for daily rhythms of behavior. ATAXIN is an RNA-binding protein and cooperates in the accumulation of the Per (Period) protein, a core transcriptional regulatory component of the clock. </jats:p>

<jats:title>ATAXIN Clock</jats:title> <jats:p> Although core components of circadian clocks in flies and mammals are transcriptional circuits, recent evidence indicates posttranscriptional regulation of the clock occurs. Studies from <jats:bold>Lim and Allada</jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="875" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1234785">875</jats:related-article> ) and <jats:bold> Zhang <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6134" page="879" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1234746">879</jats:related-article> ) converge to show that the protein ATAXIN-2, associated with neurodegenerative diseases in humans, is a regulator of translation required for normal clock function in pacemaker neurons and for daily rhythms of behavior. ATAXIN is an RNA-binding protein and cooperates in the accumulation of the Per (Period) protein, a core transcriptional regulatory component of the clock. </jats:p>

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<jats:title>CMV Breaks All the Rules</jats:title> <jats:p> One vaccine strategy being pursued against HIV is to generate protection that is dependent on cell-mediated, rather than humoral, immune responses. A cytomegalovirus (CMV)–vectored vaccine that expresses simian immunodeficiency virus (SIV) antigens exhibits stringent and durable viral control upon SIV challenge in approximately half of vaccinated rhesus macaques. <jats:bold> Hansen <jats:italic>et al.</jats:italic> </jats:bold> ( <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.1237874">10.1126/science.1237874</jats:related-article> , see the Perspective by <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6135" page="937" related-article-type="in-this-issue" vol="340" xlink:href="10.1126/science.1239649"> <jats:bold>Goonetilleke and McMichael</jats:bold> </jats:related-article> ) sought to determine the basis for the protection and discovered that the CD8 <jats:sup>+</jats:sup> T cell response in vaccinated monkeys does not target canonical SIV epitopes, which SIV is known to escape, but rather generates a broad, promiscuous response. </jats:p>