We are analyzing https://link.springer.com/article/10.1007/s10495-013-0924-5.

Title:
The DAPK family: a structure–function analysis | Apoptosis
Description:
DAP-kinase (DAPK) is the founding member of a family of highly related, death associated Ser/Thr kinases that belongs to the calmodulin (CaM)-regulated kinase superfamily. The family includes DRP-1 and ZIP-kinase (ZIPK), both of which share significant homology within the common N-terminal kinase domain, but differ in their extra-catalytic domains. Both DAPK and DRP-1 possess a conserved CaM autoregulatory domain, and are regulated by calcium-activated CaM and by an inhibitory auto-phosphorylation within the domain. ZIPK’s activity is independent of CaM but can be activated by DAPK. The three kinases share some common functions and substrates, such as induction of autophagy and phosphorylation of myosin regulatory light chain leading to membrane blebbing. Furthermore, all can function as tumor suppressors. However, they also each possess unique functions and intracellular localizations, which may arise from the divergence in structure in their respective C-termini. In this review we will introduce the DAPK family, and present a structure/function analysis for each individual member, and for the family as a whole. Emphasis will be placed on the various domains, and how they mediate interactions with additional proteins and/or regulation of kinase function.
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Keywords {🔍}

pubmed, article, google, scholar, cas, kinase, protein, kimchi, cell, dapk, biol, apoptosis, deathassociated, chen, activity, central, bialik, death, tumor, mol, dapkinase, chem, function, kinases, lin, cohen, embo, suppressor, family, shani, domain, zip, oncogene, dap, wang, research, drp, autophagy, access, berissi, kuo, activation, cells, privacy, cookies, content, phosphorylation, myosin, regulation, feinstein,

Topics {✒️}

beta-catenin-induced anoikis resistance p19arf/p53-mediated apoptotic checkpoint month download article/chapter calcium/calmodulin-dependent protein kinase tcr-stimulated nf-kappa dapk-zipk-l13a axis constitutes involve myosin-ii phosphorylation dlk/zip kinase-induced apoptosis ca2+/calmodulin-dependent dap-kinase promotes autophagy epo-dependent erythroblast formation integrin-mediated polarity pathway full il-1beta production dap-kinase-mediated morphological dlk/zip kinase leads dap-kinase induces apoptosis rsk-mediated survival signaling serine/threonine kinase involved calmodulin-calcium complexes programmed cell death e3 ubiquitin ligase serine/threonine kinases related full article pdf pro-apoptotic protein kinase par-4/dlk-mediated apoptosis dependence receptor unc5h2/ cell death-inducing functions dapk–erk interaction promote shani bialik & adi kimchi dapk-related protein kinases article apoptosis aims drp-1 gene produces tumor suppressor gene wavrant-de vrieze starvation-induced autophagy enhances neutrophil maturation ceramide-induced anoikis privacy choices/manage cookies 1007/s10495-013-0926-3 kogel dlk/zip kinase dap-kinase regulates inhibitory auto-phosphorylation death domain-binding protein zip kinase identified european research council intramolecular signalling regulate microtubule assembly conserved vertebrate gene fas-induced apoptosis serine/threonine kinase

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         description:DAP-kinase (DAPK) is the founding member of a family of highly related, death associated Ser/Thr kinases that belongs to the calmodulin (CaM)-regulated kinase superfamily. The family includes DRP-1 and ZIP-kinase (ZIPK), both of which share significant homology within the common N-terminal kinase domain, but differ in their extra-catalytic domains. Both DAPK and DRP-1 possess a conserved CaM autoregulatory domain, and are regulated by calcium-activated CaM and by an inhibitory auto-phosphorylation within the domain. ZIPK’s activity is independent of CaM but can be activated by DAPK. The three kinases share some common functions and substrates, such as induction of autophagy and phosphorylation of myosin regulatory light chain leading to membrane blebbing. Furthermore, all can function as tumor suppressors. However, they also each possess unique functions and intracellular localizations, which may arise from the divergence in structure in their respective C-termini. In this review we will introduce the DAPK family, and present a structure/function analysis for each individual member, and for the family as a whole. Emphasis will be placed on the various domains, and how they mediate interactions with additional proteins and/or regulation of kinase function.
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            Autophagy
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            Cancer Research
            Cell Biology
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            Biochemistry
            general
            Virology
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      headline:The DAPK family: a structure–function analysis
      description:DAP-kinase (DAPK) is the founding member of a family of highly related, death associated Ser/Thr kinases that belongs to the calmodulin (CaM)-regulated kinase superfamily. The family includes DRP-1 and ZIP-kinase (ZIPK), both of which share significant homology within the common N-terminal kinase domain, but differ in their extra-catalytic domains. Both DAPK and DRP-1 possess a conserved CaM autoregulatory domain, and are regulated by calcium-activated CaM and by an inhibitory auto-phosphorylation within the domain. ZIPK’s activity is independent of CaM but can be activated by DAPK. The three kinases share some common functions and substrates, such as induction of autophagy and phosphorylation of myosin regulatory light chain leading to membrane blebbing. Furthermore, all can function as tumor suppressors. However, they also each possess unique functions and intracellular localizations, which may arise from the divergence in structure in their respective C-termini. In this review we will introduce the DAPK family, and present a structure/function analysis for each individual member, and for the family as a whole. Emphasis will be placed on the various domains, and how they mediate interactions with additional proteins and/or regulation of kinase function.
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         DRP-1
         ZIP-kinase
         Programmed cell death
         Autophagy
         Ca2+-calmodulin
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
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