We are analyzing https://link.springer.com/article/10.1007/s10495-013-0926-3.

Title:
The DAP-kinase interactome | Apoptosis
Description:
DAP-kinase (DAPK) is a Ca2+/calmodulin regulated Ser/Thr kinase that activates a diverse range of cellular activities. It is subject to multiple layers of regulation involving both intramolecular signaling, and interactions with additional proteins, including other kinases and phosphatases. Its protein stability is modulated by at least three distinct ubiquitin-dependent systems. Like many kinases, DAPK participates in several signaling cascades, by phosphorylating additional kinases such as ZIP-kinase and protein kinase D (PKD), or Pin1, a phospho-directed peptidyl-prolyl isomerase that regulates the function of many phosphorylated proteins. Other substrate targets have more direct cellular effects; for example, phosphorylation of the myosin II regulatory chain and tropomyosin mediate some of DAPK’s cytoskeletal functions, including membrane blebbing during cell death and cell motility. DAPK induces distinct death pathways of apoptosis, autophagy and programmed necrosis. Among the substrates implicated in these processes, phosphorylation of PKD, Beclin 1, and the NMDA receptor has been reported. Interestingly, not all cellular effects are mediated by DAPK’s catalytic activity. For example, by virtue of protein–protein interactions alone, DAPK activates pyruvate kinase isoform M2, the microtubule affinity regulating kinases and inflammasome protein NLRP3, to promote glycolysis, influence microtubule dynamics, and enhance interleukin-1β production, respectively. In addition, a number of other substrates and interacting proteins have been identified, the physiological significance of which has not yet been established. All of these substrates, effectors and regulators together comprise the DAPK interactome. By presenting the components of the interactome network, this review will clarify both the mechanisms by which DAPK function is regulated, and by which it mediates its various cellular effects.
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Keywords {🔍}

pubmed, article, google, scholar, cas, kinase, protein, cell, dapk, biol, kimchi, deathassociated, chen, apoptosis, phosphorylation, death, chem, doijbcm, central, bialik, dapkinase, activity, tumor, function, signaling, kinases, mol, autophagy, lin, cellular, regulates, mediates, activation, cancer, research, proteins, substrates, access, signalling, embo, zhang, dap, privacy, cookies, content, regulation, sci, shohat, differ, wang,

Topics {✒️}

/ncb/journal/v14/n12/abs/ncb2629 phospho-directed peptidyl-prolyl isomerase p19arf/p53-mediated apoptotic checkpoint month download article/chapter dapk-zipk-l13a axis constitutes distinct ubiquitin-dependent systems enhance interleukin-1β production tcr-stimulated nf-kappa contraction-induced glucose uptake full il-1{beta} production caveolae/raft-mediated endocytosis sodium selenite-induced activation involve myosin-ii phosphorylation inflammatory gene expression integrin-mediated polarity pathway dap-kinase-mediated morphological stat1-mediated transcriptional activation dap-kinase induces apoptosis akt/mtor signaling pathway ribosomal protein s6 full article pdf rsk-mediated survival signaling e3 ubiquitin ligase dap-kinase-mediated phosphorylation eisenberg-lerner cell death-inducing functions article apoptosis aims dependence receptor unc5h2/ ca2+/calmodulin-dependent privacy choices/manage cookies dap kinase mediates programmed necrosis related subjects dapk–erk interaction promote death domain-binding protein european research council calmodulin-regulated death mdm2 ubiquitination signal ceramide-induced anoikis phosphorylation signalling unique kinase hierarchy colorectal tumor cells limk/cofilin complex dapk-interacting partner tnfalpha-induced apoptosis tnf-induced apoptosis prolyl isomerase activity levin-salomon ca2+-dependent phosphorylation prolyl isomerase pin1

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         description:DAP-kinase (DAPK) is a Ca2+/calmodulin regulated Ser/Thr kinase that activates a diverse range of cellular activities. It is subject to multiple layers of regulation involving both intramolecular signaling, and interactions with additional proteins, including other kinases and phosphatases. Its protein stability is modulated by at least three distinct ubiquitin-dependent systems. Like many kinases, DAPK participates in several signaling cascades, by phosphorylating additional kinases such as ZIP-kinase and protein kinase D (PKD), or Pin1, a phospho-directed peptidyl-prolyl isomerase that regulates the function of many phosphorylated proteins. Other substrate targets have more direct cellular effects; for example, phosphorylation of the myosin II regulatory chain and tropomyosin mediate some of DAPK’s cytoskeletal functions, including membrane blebbing during cell death and cell motility. DAPK induces distinct death pathways of apoptosis, autophagy and programmed necrosis. Among the substrates implicated in these processes, phosphorylation of PKD, Beclin 1, and the NMDA receptor has been reported. Interestingly, not all cellular effects are mediated by DAPK’s catalytic activity. For example, by virtue of protein–protein interactions alone, DAPK activates pyruvate kinase isoform M2, the microtubule affinity regulating kinases and inflammasome protein NLRP3, to promote glycolysis, influence microtubule dynamics, and enhance interleukin-1β production, respectively. In addition, a number of other substrates and interacting proteins have been identified, the physiological significance of which has not yet been established. All of these substrates, effectors and regulators together comprise the DAPK interactome. By presenting the components of the interactome network, this review will clarify both the mechanisms by which DAPK function is regulated, and by which it mediates its various cellular effects.
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         Phosphorylation
         Programmed cell death
         Substrates
         Interacting proteins
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
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