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<jats:title>From sensing leucine to metabolic control</jats:title> <jats:p> The mTORC1 protein kinase complex plays central roles in regulating cell growth and metabolism and is implicated in common human diseases such as diabetes and cancer. The level of the amino acid leucine tells an organism a lot about its physiological state, including how much food is available, how much insulin is going to be needed, and whether new muscle mass can be made (see the Perspective by Buel and Blenis). Wolfson <jats:italic>et al.</jats:italic> identified a biochemical sensor of leucine, Sestrin2, which connects the concentration of leucine to the control of organismal metabolism and growth. When leucine bound to Sestrin2, it was released from a complex with the mTORC1 regulatory factor GATOR2, activating the mTORC1 complex. Saxton <jats:italic>et al.</jats:italic> describe the crystal structure of Sestrin2 and show how it specifically detects leucine. Aylett <jats:italic>et al.</jats:italic> determined the structure of human mTORC1 by cryoelectron microscopy and the crystal structure of a regulatory subunit, Raptor. The results reveal the structural basis for the function and intricate regulation of this important enzyme, which is also a strategic drug target. </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="6268" page="43" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aab2674">43</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="48" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aaa3870">48</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="53" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad2087">53</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="25" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad9696">25</jats:related-article> </jats:p>

<jats:title>From sensing leucine to metabolic control</jats:title> <jats:p> The mTORC1 protein kinase complex plays central roles in regulating cell growth and metabolism and is implicated in common human diseases such as diabetes and cancer. The level of the amino acid leucine tells an organism a lot about its physiological state, including how much food is available, how much insulin is going to be needed, and whether new muscle mass can be made (see the Perspective by Buel and Blenis). Wolfson <jats:italic>et al.</jats:italic> identified a biochemical sensor of leucine, Sestrin2, which connects the concentration of leucine to the control of organismal metabolism and growth. When leucine bound to Sestrin2, it was released from a complex with the mTORC1 regulatory factor GATOR2, activating the mTORC1 complex. Saxton <jats:italic>et al.</jats:italic> describe the crystal structure of Sestrin2 and show how it specifically detects leucine. Aylett <jats:italic>et al.</jats:italic> determined the structure of human mTORC1 by cryoelectron microscopy and the crystal structure of a regulatory subunit, Raptor. The results reveal the structural basis for the function and intricate regulation of this important enzyme, which is also a strategic drug target. </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="6268" page="43" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aab2674">43</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="48" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aaa3870">48</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="53" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad2087">53</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="25" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad9696">25</jats:related-article> </jats:p>

<jats:title>From sensing leucine to metabolic control</jats:title> <jats:p> The mTORC1 protein kinase complex plays central roles in regulating cell growth and metabolism and is implicated in common human diseases such as diabetes and cancer. The level of the amino acid leucine tells an organism a lot about its physiological state, including how much food is available, how much insulin is going to be needed, and whether new muscle mass can be made (see the Perspective by Buel and Blenis). Wolfson <jats:italic>et al.</jats:italic> identified a biochemical sensor of leucine, Sestrin2, which connects the concentration of leucine to the control of organismal metabolism and growth. When leucine bound to Sestrin2, it was released from a complex with the mTORC1 regulatory factor GATOR2, activating the mTORC1 complex. Saxton <jats:italic>et al.</jats:italic> describe the crystal structure of Sestrin2 and show how it specifically detects leucine. Aylett <jats:italic>et al.</jats:italic> determined the structure of human mTORC1 by cryoelectron microscopy and the crystal structure of a regulatory subunit, Raptor. The results reveal the structural basis for the function and intricate regulation of this important enzyme, which is also a strategic drug target. </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="6268" page="43" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aab2674">43</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="48" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aaa3870">48</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="53" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad2087">53</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6268" page="25" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad9696">25</jats:related-article> </jats:p>

<jats:title>Printing ceramics into complex shapes</jats:title> <jats:p> Some materials, such as thermoplastics and metals, are naturally suited to being 3D printed because the individual particles can be fused together by applying heat. In contrast, ceramics do not fuse together the same way. Eckel <jats:italic>et al.</jats:italic> developed a way to pattern specific preceramic monomers using either 3D printing or stereolithography into complex, curved, and porous shapes. Upon heating, they observed almost no shrinkage, and the formed parts showed exceptional thermal stability. </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="6268" page="58" related-article-type="in-this-issue" vol="351" xlink:href="10.1126/science.aad2688">58</jats:related-article> </jats:p>