Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 40, Issue -, Pages 1052-1057Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20120155
Keywords
autophagy; autophosphorylation; DAPK (death-associated protein kinase); leucine-rich repeat kinase 2 (LRRK2)
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Funding
- Merck-Serono
- Center of Excellence grant from Flight Attendant Medical Research Institute (FAMRI)
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DAPK (death-associated protein kinase) is a newly recognized member of the mammalian family of ROCO proteins, characterized by common ROC (Ras of complex proteins) and COR (C-terminal of ROC) domains. In the present paper, we review our recent work showing that DAPK is functionally a ROCO protein; its ROC domain binds and hydrolyses GTP. Furthermore, GTP binding regulates DAPK catalytic activity in a novel manner by enhancing autophosphorylation on inhibitory Ser(308), thereby promoting the kinase 'off' state. This is a novel mechanism for in cis regulation of kinase activity by the distal ROC domain. The functional similarities between DAPK and the Parkinson's disease-associated protein LRRK2 (leucine-rich repeat protein kinase 2), another member of the ROCO family, are also discussed.
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