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Cover Figure

ONLINE COVER This week's issue features a Research Article in which a mutant form of the atypical protein kinase CASK [calcium/calmodulin (CaM)–activated serine-threonine kinase] was used to investigate the role of Mg2+ in facilitating kinase catalytic activity. Phylogenetic analyses indicated that CASK, which—unlike conventional kinases—doesn't require Mg2+ for its catalytic activity, evolved from a Mg2+-dependent kinase and suggested that CASK's loss of Mg2+-dependent catalytic activity may have enabled the development of a mechanism through which it could be regulated by localized changes in divalent cation concentration. The image shows the crystal structure of CASK in the foreground (PDB: 3C0H) and a typical calcium/calmodulin-regulated kinase, CaMKII, in the background (PDB: 2BDW). [Image: Chris Bickel, AAAS]

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Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882