Journal
CELL
Volume 133, Issue 2, Pages 204-205Publisher
CELL PRESS
DOI: 10.1016/j.cell.2008.04.005
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM019301] Funding Source: Medline
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Pseudokinases lack conservation of one or more of the catalytic residues in the kinase core and as a consequence are typically thought to be catalytically inactive. New work by Mukherjee et al. (2008) challenges this assumption. They show that the pseudokinase domain of CASK ( Ca2+/calmodulin activated serine-threonine kinase) adopts an active conformation and displays catalytic activity in vivo.
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