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promoting ER stress-ATF6-DAPK1 signaling in transporting enterocytes counters the transcellular passage of bacteria evoked by dysfunctional mitochondria
DAPK deficiency leads to excess HIF-1a accumulation, enhanced IL-17 expression and exacerbated experimental autoimmune encephalomyelitis.
Excitotoxicity can proceed without increased Ser-1303 phosphorylation, and is unaffected by Dapk1 deficiency in vitro or following ischemia in vivo.
Authors find that the LTP specificity of CaMKII synaptic accumulation is due to its LTD-specific suppression by calcineurin (CaN)-dependent DAPK1 activation, which in turn blocks CaMKII binding to GluN2B.
DAPK1 specifically phosphorylates NDRG2 Ser350 and this phosphorylation is an important caspase-dependent mechanism by which NDRG2 mediates cell death in neuronal cells.
Inhibition of DAPK1 by deleting a catalytic domain or a death domain of DAPK1 rescues the Excitatory pyramidal neurons in the entorhinal cortical layer II region synaptic loss
in Alzheimer's disease (AD) brains, elevated DAPK1 levels showed co-relation with the increase of APP phosphorylation. Combined together, these results suggest that DAPK1 promotes the phosphorylation and amyloidogenic processing of APP, and that may serve a potential therapeutic target for AD.
This study demonstrate that phosphorylation of Tau at Serine 262 by the kinase domain of DAPK1 mediates spine damage and the subsequent neuronal death in ischemic stroke.
DAPK1-p53 interaction is a preferred target for therapeutic intervention of stroke.
Suggest that DAPK1 is a novel regulator of tau protein abundance, and that DAPK1 upregulation might contribute to tau-related pathologies in Alzheimer disease.
the DAPK1-p53 interaction is a signaling point of convergence of necrotic and apoptotic pathways
TSC2 binds to the death domain of DAPK. This interaction is required for TSC2 to reduce DAPK protein levels and half-life. DAPK is regulated by the lysosome pathway. Lysosome inhibition blocks TSC2-mediated degradation of DAPK.
Results identify DAPK as a molecule required for full production of IL-1beta and functional assembly of the NLRP3 inflammasome.
Study reports that cerebral ischemia recruits death-associated protein kinase 1 (DAPK1) into the NMDA receptor NR2B protein complex in the cortex of adult mice.
Death-associated protein kinase (DAPK) is regulated by DANGER which binds directly to DAPK and inhibits catalytic activity.
cellular activities of DAPK are critical for antagonizing caspase-dependent apoptosis to promote cell survival under normal cell growth conditions.
DAPK has a role in tubular cell apoptosis and renal dysfunction after IR injury
kinase domain of Dapk1 deleted by gene targeting plays a suppressive role for the development of renal fibrosis through inhibition of the tubular epithelial-to-mesenchymal transition in a mouse model of chronic obstructive uropathy
Results revealed crucial implications of DAPK in regulating spatial memory.
show a critical role for C/EBP-beta in a novel IFN-induced cell growth-suppressive pathway via DAPK1
DAPK1 methylation level is associated with gliomas clinical features and outcomes
LncRNA MIR22HG could act as a tumor suppressor and inhibited EC cells proliferation through regulating miR-141-3p/DAPK1 axis.
Our results showed that DAPK promoter methylation is tightly correlated with clinicopathological features of NSCLC and is associated with poor prognosis in patients.
High Promoter Methylation of DAPK1 gene is associated with Breast Cancer.
It is this DAPK1-NR2B interaction that arbitrates the pathological processes like apoptosis, necrosis, and autophagy of neuronal cells observed in stroke injury, hence we aimed to inhibit this vital interaction to prevent neuronal damage.
DNA hypermethylation of DAPK1 gene promoter is a promising biomarker for OSCC prediction/prognostics
rs4878104 T allele could significantly regulate increased DAPK1 expression in European population
the DAPK-mTOR pathway is critical for anti-HCV effects of peg-IFN-alpha
A significant correlation between changes in the levels of expression and methylation was detected for the three apoptosis-regulatory genes (APAF1, DAPK1, and BCL2). The results suggest that methylation play an important role in the regulation of the apoptosis system genes in breast cancer.
Results show that DNA demethylation of distinct promoter regions is associated with re-expression of the tumor suppressor gene DAPK1. Its knockdown promotes tumor cell migration in breast cancer cell line.
Data show that silencing DNA methyltransferase 1 (DNMT1) increased expression of tumor suppressor genes, RASSF1A and DAPK, in esophageal squamous cell carcinoma (ESCC) cells and ESCC xenograft in nude mice.
The current study supports a relevant role for p15, p16, and DAPK hypermethylation in the genesis of the plasma cell neoplasm. DAPK hypermethylation also might be an important step in the progression from MGUS to MM.
DAPK1 methylation is associated with the risk of gastrointestinal cancer.
downregulation of HOXC9 releases its transcriptional inhibition of DAPK1, resulting in the activation of the DAPK1-Beclin1 pathway, which induces autophagy in glioblastoma cells
findings evidence a positive correlation between SIRT1 and BCL6 expression increase in follicular lymphomas (FL) . SIRT1 methylation decreases in FL and diffuse large-B cell lymphomas (DLBCL)and this parallels the increase of KLF4, DAPK1 and SPG20 methylation
results suggest that DAPK1 is an important prognostic marker and therapeutic target for bladder cancer and have identified possible therapeutic agents for future testing in bladder cancer models with low DAPK1 expression
Study provides evidence that DAPK1 is a negative-feedback regulator of the RIG-I pathway. RIG-I-mediated antiviral signaling activates DAPK1 kinase activity and DAPK1 inactivates RIG-I RNA sensing by direct phosphorylation of RIG-I.
Meta-analysis suggested that aberrant methylation of DAPK promoter was associated with head and neck squamous cell carcinoma.
Death-associated protein kinase 1 is a positive mediator of gamma-interferon induced programmed cell death. DAPK1 encodes a structurally unique 160-kD calmodulin dependent serine-threonine kinase that carries 8 ankyrin repeats and 2 putative P-loop consensus sites. It is a tumor suppressor candidate.
death-associated protein kinase 1
, death-associated protein kinase 1-like
, DAP kinase 1