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]

[Table of Contents]

To Advertise   |   Find Products