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dc.contributor.authorCarlessi, Rodrigo
dc.contributor.authorLevin-Salomon, V.
dc.contributor.authorCiprut, S.
dc.contributor.authorBialik, S.
dc.contributor.authorBerissi, H.
dc.contributor.authorAlbeck, S.
dc.contributor.authorPeleg, Y.
dc.contributor.authorKimchi, A.
dc.identifier.citationCarlessi, R. and Levin-Salomon, V. and Ciprut, S. and Bialik, S. and Berissi, H. and Albeck, S. and Peleg, Y. et al. 2011. GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling. EMBO Reports. 12 (9): pp. 917-923.

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. © 2011 European Molecular Biology Organization.

dc.titleGTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling
dc.typeJournal Article
dcterms.source.titleEMBO Reports
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusOpen access via publisher

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