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dapk, ser, ampk, phosphorylation, cells, kinase, pubmed, article, autophagy, beclin, google, scholar, cam, protein, fig, cas, cell, binding, activation, catalytic, assay, transfected, activity, performed, domain, mutant, central, incubated, flagdapk, buffer, hekt, sirna, nature, phosphorylated, control, shown, treated, biol, proteins, mutants, mlc, site, response, experiments, metabolic, autophosphorylation, independent, thr, test, sdspage,

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nature portfolio privacy policy beta-catenin-induced anoikis resistance hrp-conjugated goat anti-mouse thermo fisher scientific advertising nature including development regulated ser/thr kinase8 social media cdna library european research council cancer research chemical research support reprints edta-free protease-inhibitor tablet anti-rabbit secondary antibodies s289d phospho-mimicking mutant autophagy research ion-trap mass spectrometer cgmp-dependent protein kinase auto-regulatory domain binds puncta area/cell area cam auto-regulatory domain39 cam auto-regulatory domains9 exploratory research sqstm1-dependent selective autophagy central metabolic sensor calmodulin-regulated protein kinase beclin-1/atg14/vps34 complex activity protein-fragment complementation assays inhibitory auto-regulatory domain dfcp1-gfp puncta specifically cam auto-regulatory domain phospho-silencing mutant s289a hek293 gfp-lc3b cells cam auto-regulatory domains blocking access double-membrane autophagic vesicles18 discovering protein–protein interactions protein-fragment complementation screen k42a s289a double-mutant coupled calcium/calmodulin binding ser289 phospho-mimicking mutants epo-dependent erythroblast formation author information authors dap-kinase promotes autophagy amp-activated protein kinase a549-dfcp1-gfp cells a549 dfcp1-gfp cells

Questions {❓}

• AMPK as a mediator of tissue preservation: time for a shift in dogma?

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      description:Autophagy is an intracellular degradation process essential for adaptation to metabolic stress. DAPK2 is a calmodulin-regulated protein kinase, which has been implicated in autophagy regulation, though the mechanism is unclear. Here, we show that the central metabolic sensor, AMPK, phosphorylates DAPK2 at a critical site in the protein structure, between the catalytic and the calmodulin-binding domains. This phosphorylation activates DAPK2 by functionally mimicking calmodulin binding and mitigating an inhibitory autophosphorylation, providing a novel, alternative mechanism for DAPK2 activation during metabolic stress. In addition, we show that DAPK2 phosphorylates the core autophagic machinery protein, Beclin-1, leading to dissociation of its inhibitor, Bcl-XL. Importantly, phosphorylation of DAPK2 by AMPK enhances DAPK2’s ability to phosphorylate Beclin-1, and depletion of DAPK2 reduces autophagy in response to AMPK activation. Our study reveals a unique calmodulin-independent mechanism for DAPK2 activation, critical to its function as a novel downstream effector of AMPK in autophagy. DAPK2 is a calmodulin-regulated protein kinase implicated in autophagy regulation, but how physiological stress leads to its activation is yet unknown. Here, the authors show that the central metabolic sensor AMPK phosphorylates DAPK2 to promote autophagy in a calmodulin-independent mechanism.
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