Beschreibung:
<jats:title>Lipid Kinase Revealed</jats:title>
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The lipid kinase, Vps34, makes the key signaling lipid phosphatidylinositol 3-phosphate [PI(3)P] and has essential roles in autophagy, membrane trafficking, and cell signaling. It is a class III PI 3-kinase, a class against which there is currently no specific inhibitor.
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Miller
<jats:italic>et al.</jats:italic>
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(p.
<jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" page="1638" related-article-type="in-this-issue" vol="327" xlink:href="10.1126/science.1184429">1638</jats:related-article>
) now describe the crystal structure of Vps34. Modeling substrate binding and combining structural data with mutagenesis suggests a mechanism in which Vps34 is auto-inhibited in solution, but adopts a catalytically active conformation on membranes. Structures of Vps34 with existing inhibitors might allow for the generation of inhibitors with high affinity and specificity.
</jats:p>