Journal
EMBO REPORTS
Volume 12, Issue 9, Pages 917-923Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/embor.2011.126
Keywords
GTP-binding proteins; DAP-kinase; ROCO family; LRRK2
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Funding
- Merck-Serono
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Death-associated protein kinase (DAPk) was recently suggested by sequence homology to be a member of the ROCO family of proteins. Here, we show that DAPk has a functional ROC (Ras of complex proteins) domain that mediates homo-oligomerization and GTP binding through a defined P-loop motif. Upon binding to GTP, the ROC domain negatively regulates the catalytic activity of DAPk and its cellular effects. Mechanistically, GTP binding enhances an inhibitory autophosphorylation at a distal site that suppresses kinase activity. This study presents a new mechanism of intramolecular signal transduction, by which GTP binding operates in cis to affect the catalytic activity of a distal domain in the protein.
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