| pubmed-article:9118961 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9118961 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:9118961 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:9118961 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9118961 | lifeskim:mentions | umls-concept:C1264638 | lld:lifeskim |
| pubmed-article:9118961 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:9118961 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:9118961 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9118961 | pubmed:dateCreated | 1997-4-22 | lld:pubmed |
| pubmed-article:9118961 | pubmed:abstractText | DAP-kinase was initially identified as a gene whose anti-sense-mediated reduced expression protected HeLa cells from interferon-gamma-induced programmed cell death. It was cloned in our laboratory by a functional gene selection approach. According to its amino acid sequence, this 160 kDa protein was predicted to be a novel type of calmodulin-regulated serine/threonine kinase which carries ankyrin repeats and the death domain. In this work we have shown that the kinase was autophosphorylated and capable of phosphorylating an exogenous substrate in a Ca2+/calmodulin-dependent manner. We proved that calmodulin binds directly to the recombinant kinase, and generated a constitutively active kinase mutant by the deletion of the calmodulin-regulatory domain. By immunostaining and biochemical fractionations we demonstrated that the kinase is localized to the cytoskeleton, in association with the microfilament system, and mapped a region within the protein which is responsible for binding to the cytoskeleton. Several assays attributed a cell death function to the gene. Ectopic expression of wild-type DAP-kinase induced the death of target cells, and the killing property depended strictly on the status of the intrinsic kinase activity. Conversely, a catalytically inactive mutant that carried a lysine to alanine substitution within the kinase domain, displayed dominant-negative features and protected cells from interferon-gamma-induced cell death. DAP-kinase is therefore a novel cytoskeletal-associated cell death serine/threonine kinase whose activation by Ca2+/calmodulin may be linked to the biochemical mechanism underlying the cytoskeletal alterations that occur during cell death. | lld:pubmed |
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| pubmed-article:9118961 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9118961 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9118961 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9118961 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9118961 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9118961 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9118961 | pubmed:author | pubmed-author:KinskyC BCB | lld:pubmed |
| pubmed-article:9118961 | pubmed:author | pubmed-author:CohenOO | lld:pubmed |
| pubmed-article:9118961 | pubmed:author | pubmed-author:FeinsteinEE | lld:pubmed |
| pubmed-article:9118961 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9118961 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:9118961 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9118961 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9118961 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9118961 | pubmed:pagination | 998-1008 | lld:pubmed |
| pubmed-article:9118961 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:9118961 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9118961 | pubmed:articleTitle | DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. | lld:pubmed |
| pubmed-article:9118961 | pubmed:affiliation | Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot, Israel. | lld:pubmed |
| pubmed-article:9118961 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9118961 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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