Cited by 495Neuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration MechanismsAcute Ischemic Stroke Management

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DAPK1 Interaction with NMDA Receptor NR2B Subunits Mediates Brain Damage in Stroke

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Tu, Weihong, Xu, Xin, Peng, Lisheng, Zhong, Xiaofen, Zhang, Wenfeng, Soundarapandian, Mangala M., Belal, Cherine, Wang, Manqi, Jia, Nali, Zhang, Wen, Lew, Frank, Chan, Sic Lung, Chen, Yanfang, Lu, Youming·2010·Cell

DOI 10.1016/j.cell.2009.12.055PMC PMC2820131

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Abstract

N-methyl-D-aspartate (NMDA) receptors constitute a major subtype of glutamate receptors at extrasynaptic sites that link multiple intracellular catabolic processes responsible for irreversible neuronal death. Here, we report that cerebral ischemia recruits death-associated protein kinase 1 (DAPK1) into the NMDA receptor NR2B protein complex in the cortex of adult mice. DAPK1 directly binds with the NMDA receptor NR2B C-terminal tail consisting of amino acid 1292-1304 (NR2B(CT)). A constitutively active DAPK1 phosphorylates NR2B subunit at Ser-1303 and in turn enhances the NR1/NR2B receptor channel conductance. Genetic deletion of DAPK1 or administration of NR2B(CT) that uncouples an activated DAPK1 from an NMDA receptor NR2B subunit in vivo in mice blocks injurious Ca(2+) influx through NMDA receptor channels at extrasynaptic sites and protects neurons against cerebral ischemic insults. Thus, DAPK1 physically and functionally interacts with the NMDA receptor NR2B subunit at extrasynaptic sites and this interaction acts as a central mediator for stroke damage.

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Quillinan, N., Grewal, H., Deng, G., Shimizu, K., Yonchek, J. C., Strnad, F. A., Traystman, R. J., & Herson, P. S. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.10.033 · Cited by 24
“Specifically, GluN2A couples to cAMP response element-binding (CREB) phosphorylation and activation while GluN2B opposes CREB activation and signals to death-associated protein kinase (DAPK) (Hardingham et al., 2002; Tu et al., 2010).”
The Role of GluN2A in Cerebral Ischemia: Promoting Neuron Death and Survival in the Early Stage and Thereafter
Sun, Y., Cheng, X., Hu, J. H., & Gao, Z. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0395-8 · Cited by 24
Pituitary Adenylate Cyclase Activating Polypeptide Elicits Neuroprotection Against Acute Ischemic Neuronal Cell Death Associated with NMDA Receptors
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Novel Synthesis and Characterization of Doxycycline‐Loaded Gold Nanoparticles: The Golden Doxycycline for Antibacterial Applications
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TRPC6 Inhibited NMDA Current in Cultured Hippocampal Neurons
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Kinesin-1 Regulates Extrasynaptic Targeting of NMDARs and Neuronal Vulnerability Toward Excitotoxicity
Lin, R., Duan, Z., Sun, H., Fung, M.-L., Chen, H., Wang, J., Lau, C. G., Yang, D., Liu, Y., Ni, Y., et al. (2019) · iScience · doi:10.1016/j.isci.2019.02.009 · Cited by 23
Traditional Chinese medicines treat ischemic stroke and their main bioactive constituents and mechanisms
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“NMDAR hyperactivation promotes calcium inward flow and stimulates calcineurin, which then dephosphorylates and activates DAPK1, which is then moved to the neighborhood of NMDAR2B to aggravate ischemia injury (Tu et al., 2010).”
Background
NMDAR-Mediated Hippocampal Neuronal Death is Exacerbated by Activities of ASIC1a
Gao, S., Yang, Y., Ma, Z., Sun, H. Q., Zhang, Y., Wang, X.-T., Wang, C., Fan, W.-M., Zheng, Q., & Ma, C. (2015) · Neurotoxicity Research · doi:10.1007/s12640-015-9530-3 · Cited by 23
“Since the phosphorylation of NR2B subunits of the NMDAR was well known to correlate with cell death (Tu et al. 2010; Lai et al. 2014), we examined whether activation of ASIC1a resulted in an increase in NR2B phosphorylation.”
Changes in synaptic plasticity and expression of glutamate receptor subunits in the CA1 and CA3 areas of the hippocampus after transient global ischemia
Han, X.-J., Shi, Z., Xia, L.-X., Zhu, L.-H., Zeng, L., Nie, J., Xu, Z., & Ruan, Y. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.04.011 · Cited by 24
“However, stimulating extrasynaptic NR2B can trigger the CREB shut-off pathway and activate apoptotic pathway, prompting the interaction with death-associated protein kinase 1 (DAPK1), Ca/calmodulin (CaM)-dependent protein kinase II (CaMKII) and protein kinase A (PKA), ultimately culminating in neuronal death (Wahl et…”
Selective Regulation of NR2B by Protein Phosphatase-1 for the Control of the NMDA Receptor in Neuroprotection
Farinelli, M., Heitz, F. D., Grewe, B. F., Tyagarajan, S. K., Helmchen, F., & Mansuy, I. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034047 · Cited by 23
“Protein phosphorylation is a post-translational modification that constitutes one of the major modes of regulation of the NMDAR. Phosphorylation controls the functional properties of NMDARs and the surface expression of NMDAR subunits (Lee 2006, Salter 2004, Prybylowski 2004). While several protein kinases are known t…”
Background
Malic enzyme 2 maintains metabolic state and anti-tumor immunity of CD8+ T cells
Zhang, Z., Yang, Y., Chen, Y., Su, J., & Du, W. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.07.021 · Cited by 23
Self-citation
Characterisation of neuroprotective efficacy of modified poly-arginine-9 (R9) peptides using a neuronal glutamic acid excitotoxicity model
Edwards, A. B., Anderton, R. S., Knuckey, N. W., & Meloni, B. P. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2882-z · Cited by 24
Blocking ERK-DAPK1 Axis Attenuates Glutamate Excitotoxicity in Epilepsy
Gan, C., Zou, Y., Chen, D., Shui, X., Hu, L., Li, R., Zhang, T., Wang, J., Mei, Y., Wang, L., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126370 · Cited by 22
“Moreover, the activation of DAPK1 was confirmed by the phosphorylation of myosin light chain (MLC), a well-known DAPK1 substrate (Figure 1A,F,G,L) [32,45].”
Background
The Weakened Interaction Between HECTD4 and GluN2B in Ischemic Stroke Promotes Calcium Overload and Brain Injury Through a Mechanism Involving the Decrease of GluN2B and MALT1 Ubiquitination
Zhang, Y., Yang, X.-Y., Liu, H., Zhang, Z., Hu, C., Peng, J., & Luo, X. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03169-8 · Cited by 22
Cul3-KLHL20 ubiquitin ligase: physiological functions, stress responses, and disease implications
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“Originally discovered as a mediator of interferon-γ (IFN-γ)induced cell death [25], DAPK is subsequently found to function as a positive regulator of apoptosis in response to a wide range of stimuli, such as TNF-α, Fas [26], TGF-β [27], ceramide [28], oncogene activation [29], unligated netrin receptor [30, 31], matri…”
Background
CaMKII-mediated phosphorylation of GluN2B regulates recombinant NMDA receptor currents in a chloride-dependent manner
Tavalin, S. J., & Colbran, R. J. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2016.12.002 · Cited by 22
“While Ser1303 phosphorylation by PKC and DAPK1was shown to enhance NMDA receptor currents (Liao et al., 2001; Tu et al., 2010), the co-expression of CaMKII was reported to attenuate GluN1A/GluN2B currents by enhancing the extent”
Presynaptic Caytaxin prevents apoptosis via deactivating DAPK1 in the acute phase of cerebral ischemic stroke
Wang, S., Chen, K., Jia, Y., Wang, X., Li, Q., Lv, F., Shen, H., & Pei, L. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113303 · Cited by 22
Protection of Pyruvate against Glutamate Excitotoxicity Is Mediated by Regulating DAPK1 Protein Complex
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Regulation of Synaptic NMDA Receptor Activity by Post-Translational Modifications
Tahiri, E., Corti, E., & Duarte, C. B. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04346-6 · Cited by 22
“…of the investigators in the field of stroke since a peptide that prevents the interaction of the kinase with GluN2B protected brain damage induced by middle cerebral artery occlusion (MCAO), a model of focal brain ischemia, without affecting the physiologi - cal activation of NMDAR [85, 86 ].”
Genetic, Structural, and Molecular Insights into the Function of Ras of Complex Proteins Domains
Civiero, L., Dihanich, S., Lewis, P. A., & Greggio, E. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.05.010 · Cited by 22
Regulation of snoRNAs in Cancer: Close Encounters with Interferon
Nallar, S. C., & Kalvakolanu, D. V. (2013) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2012.0106 · Cited by 21
Fashioning drugs for stroke
Lai, T. W., & Wang, Y. T. (2010) · Nature Medicine · doi:10.1038/nm1210-1376 · Cited by 21
Enolase1 Alleviates Cerebral Ischemia-Induced Neuronal Injury via Its Enzymatic Product Phosphoenolpyruvate
Jiang, W., Tian, X., Yang, P. H., Li, J., Xiao, L., Liu, J., Liu, C., Tan, W., & Tu, H. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00103 · Cited by 18
Icaritin Alleviates Glutamate-Induced Neuronal Damage by Inactivating GluN2B-Containing NMDARs Through the ERK/DAPK1 Pathway
Liu, S., Liu, C., Xiong, L., Xie, J., Huang, C., Pi, R., Huang, Z., & Li, L. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.525615 · Cited by 22
EPAC Inhibition of SUR1 Receptor Increases Glutamate Release and Seizure Vulnerability
Zhao, K., Wen, R., Wang, X., Pei, L., Yang, Y., Shang, Y., Bazan, N. G., Zhu, L., Tian, Q., & Lu, Y. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5686-12.2013 · Cited by 21
“Whole-cell patch– clamp recordings (5 M ) at voltage– clamp mode were visualized with infrared differential interference contrast using an Axioskop 2FS equipped with Hamamatsu C2400 – 07E optics, as described previously (Peng et al., 2006; Tu et al., 2010; Yang et al., 2012).”
MethodSelf-citation
Research Advances in Chaperone-Mediated Autophagy (CMA) and CMA-Based Protein Degraders
Pan, Z., Huang, X., Liu, M., Jiang, X. L., & He, G. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02681 · Cited by 21
Death Associated Protein Kinase (DAPK) -mediated neurodegenerative mechanisms in nematode excitotoxicity
Rosario, J. S. D., Feldmann, K. G., Ahmed, T., Amjad, U., Ko, B., An, J., Mahmud, T., Salama, M., Mei, S., Asemota, D. E., et al. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0158-2 · Cited by 20
“The most cited suggestion in the field attributes the involvement of DAPK in excitotoxicity to the potentiation of Ca2+ currents through NR2B/GluN2B subunit-containing complexes of the NMDA- receptor (NMDA-Rs) family of GluRs [24].”
BackgroundInfluential
Pathophysiology of Ischemic Stroke
Li, Y., & Yang, G.-Y. (2017) · Translational medicine research · doi:10.1007/978-981-10-5804-2_4 · Cited by 22
NMDA Receptor C-Terminal Domain Signalling in Development, Maturity, and Disease
Haddow, K., Kind, P. C., & Hardingham, G. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911392 · Cited by 22
“[103] demonstrated a neuroprotective effect by using a peptide mimetic of S1303, Tat-NR2BCT, to uncouple CTD2B-DAPK1 interaction.”
BackgroundMethodResultInfluential
Carnosic Acid Attenuates AβOs-Induced Apoptosis and Synaptic Impairment via Regulating NMDAR2B and Its Downstream Cascades in SH-SY5Y Cells
Liu, W., Li, Y., Li, Y., Xu, L., & Jia, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03032-w · Cited by 20
The protective effect of polyethylene glycol-conjugated urokinase nanogels in rat models of ischemic stroke when administrated outside the usual time window
Cui, W., Liu, R., Jin, H., Huang, Y., Liu, W., & He, M. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.032 · Cited by 20
The Genetics of Alzheimer’s Disease in the Chinese Population
Gan, C., Zhang, T., & Lee, T. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072381 · Cited by 21
Biochemical and functional characterization of the ROC domain of DAPK establishes a new paradigm of GTP regulation in ROCO proteins
Bialik, S., & Kimchi, A. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120155 · Cited by 20
Exclusive Association of p53 Mutation with Super-High Methylation of Tumor Suppressor Genes in the p53 Pathway in a Unique Gastric Cancer Phenotype
Waraya, M., Yamashita, K., Ema, A., Katada, N., Kikuchi, S., & Watanabe, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139902 · Cited by 20
A Dual Role of ATM in Ischemic Preconditioning and Ischemic Injury
Xie, G.-H., Dai, H., Liu, F., Zhang, Y., Zhu, L., Nie, J.-J., & Wu, J.-H. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00773-6 · Cited by 19
Synaptic dysfunction of Aldh1a1 neurons in the ventral tegmental area causes impulsive behaviors
Li, X., Chen, W., Huang, X., Jing, W., Zhang, T., Yu, Q., Yu, H., Li, H., Tian, Q., Ding, Y., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00494-9 · Cited by 23
Self-citation
Neurodegenerative effect of DAPK1 after cerebral hypoxia-ischemia is associated with its post-transcriptional and signal transduction regulations: A systematic review and meta-analysis
Khan, Z. A., Sumsuzzman, D. M., Choi, J., & Hong, Y. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101593 · Cited by 19
“, 2010), and eight used different DAPK1 inhibition methods (Feng et al., 2020; Pei et al., 2015; Shamloo et al., 2005; Tu et al., 2010; Wang et al., 2020, 2014; Wei et al., 2019; Zhang et al., 2020) to assess its protective role after ischemia.”
BackgroundMethodInfluential
NMDA Receptor GluN2B Subunit Is Involved in Excitotoxicity Mediated by Death-Associated Protein Kinase 1 in Alzheimer’s Disease
Xu, L., Li, B., Li, F., Li, Y., Qin, W., Zhao, Y., & Jia, J. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220747 · Cited by 20
“DAPK1 is implicated in several central nervous system (CNS) diseases, including stroke [12], and depression [13], possibly due to DAPK1 relate to synaptic plasticity [14].”
Synaptotagmin-3 interactions with GluA2 mediate brain damage and impair functional recovery in stroke
Lu, H., Chen, S., Nie, Q., Xue, Q., Fan, H., Wang, Y., Fan, S., Zhu, J., Shen, H., Li, H., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112233 · Cited by 19
Aerobic exercise mitigates hippocampal neuronal apoptosis by regulating DAPK1 / CDKN2A / REDD1 / FoXO1 / FasL signaling pathway in D‐galactose‐induced aging mice
Liu, Y., Guo, W., & Hong, S. (2023) · The FASEB Journal · doi:10.1096/fj.202300847rr · Cited by 19
Long-Distance Signaling from Synapse to Nucleus via Protein Messengers
Karpova, A., Bär, J., & Kreutz, M. R. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-3-7091-0932-8_16 · Cited by 19
New Modularity of DAP-Kinases: Alternative Splicing of the DRP-1 Gene Produces a ZIPk-Like Isoform
Shoval, Y., Berissi, H., Kimchi, A., & Pietrokovski, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017344 · Cited by 19
“. DAPk is involved in several pathways leading to cell death, including apoptosis, autophagy and anoikis-like cell death. It mediates several types of stress signals induced by IFN-γ TNF-α, Fas, TGF-β, ceramides, deprivation of neuronal cells from Netrin-1, and stimulation of NMDA receptors in cerebral ischemia”
The role of DAPK–BimEL pathway in neuronal death induced by oxygen–glucose deprivation
He, C., Stroink, A. R., & Wang, C. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.11.024 · Cited by 19
“DAPK knockout mice show dramatic reduction in infarct volume and improved neurological function following cerebral ischemia (Tu et al. 2010).”
Background
A novel method using ambient glutamate for the electrophysiological quantification of extrasynaptic NMDA receptor function in acute brain slices
Moldavski, A., Behr, J., Bading, H., & Bengtson, C. P. (2019) · The Journal of Physiology · doi:10.1113/jp278362 · Cited by 18
“The pathological activation of ES-NMDARs by ambient glutamate in energy deprivation and conditions such as stroke (Jabaudon et al. 2000; Stanika et al. 2009; Tu et al. 2010; Suarez-Pinilla et al. 2014) is believed to arise from the reverse function of glutamate uptake by glia whose normal physiological function is to…”
Background

Authors: Tu, W., Xu, X., Peng, L., Zhong, X., Zhang, W., Soundarapandian, M. M., Belal, C., Wang, M., Jia, N., Zhang, W., Lew, F., Chan, S. L., Chen, Y., & Lu, Y.
Affiliations: University of Central Florida (US)
Louisiana State University (US)
Wright State University (US)
Corresponding author: Lu, Youming
ORCID: Xu, Xin
Peng, Lisheng
Zhong, Xiaofen
Zhang, Wen
Chen, Yanfang
Lu, Youming
Venue: Cell
Publisher: Elsevier BV
Published: 2010-01
Volume: 140
Issue: 2
Pages: 222-234
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2009.12.055
PMC: PMC2820131
OpenAlex: W2112215250
Cited by: 493
References: 54
Citations by year: 2026: 15 · 2025: 27 · 2024: 24 · 2023: 37 · 2022: 28 · 2021: 38 · 2020: 35 · 2019: 24 · 2018: 35 · 2017: 45 · 2016: 35 · 2015: 20 · 2014: 35 · 2013: 34 · 2012: 21
FWCI: 12.14
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1293 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Digital Commons - East Tennessee State University (East Tennessee State University) (submittedVersion)
Journal of International Crisis and Risk Communication Research (submittedVersion)
Funders: National Institute on Aging (R01AG033282YL, R01AG033282)
National Institute of Neurological Disorders and Stroke (R01NS5051383YL, R01NS051383)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Clinical Neurology › Acute Ischemic Stroke Management
Keywords: DAPK1, NMDA receptor, NR2B subunit, cerebral ischemia, stroke, extrasynaptic NMDA receptors, neuronal cell death, calcium influx, protein phosphorylation, neuroprotection
MeSH terms: Animals, Brain, Brain Ischemia, Neurons, Peptides, Recombinant Proteins, Receptors, N-Methyl-D-Aspartate, Cell Death, Calcium-Calmodulin-Dependent Protein Kinases, Stroke, Apoptosis Regulatory Proteins, Mice, tat Gene Products, Human Immunodeficiency Virus, Death-Associated Protein Kinases

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DAPK1 Interaction with NMDA Receptor NR2B Subunits Mediates Brain Damage in Stroke

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