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DAPK1 Interaction with NMDA Receptor NR2B Subunits Mediates Brain Damage in Stroke
Open accessAbstract
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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“Phosphorylation of S1303 in heterologous cells enhances NMDAR current (127, 128)”
From Synaptic memory and CaMKII (2023) · cites this paper as [128]
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“DAPK1 (FC = 1.08, p = 0.05) is a calcium-dependent serine/threonine kinase that is highly expressed in the cortex in AD [167], after ischemic damage [154], and in physiological ageing where it has been suggested to play a role in the decay of learning and memory with age [51].”
From Early onset senescence and cognitive impairment in a murine model of repeated mTBI (2021) · cites this paper as [154]
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Impact of open channel blockers on the surface dynamics and organization of NMDA receptors
Fernandes, A. (2020) · theses.fr (ABES) · doi:10.70675/d12c14b2z7a80z4668z9c48z8e2c0e41c009 · Cited by 1
Molecular mechanisms underlying the surface organization of the NMDA receptors during development
Bénac, N. (2024) · theses.fr (ABES) · doi:10.70675/e3508a2ezb62ez4f99zb27bz156201271974
NMDA Receptor Mediated Mechanisms in the Post-Stroke Brain: From Physiology to Pathology
Gong, H., Wang, X.-Z., Liu, D., Liu, W.-J., Xiaoxia, D., & Rao, J. (2026) · Biomolecules · doi:10.3390/biom16060770
“Ischemia promotes the recruitment of DAPK1 to the GluN2B CTD [54], resulting in phosphorylation at Ser1303 and amplification of neurotoxic signaling [55].”
Death-associated protein kinase 1 in neurodegenerative disorders
Pandey, S. K., Singh, S., Shukla, S., & Singh, R. K. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44173-8.00017-6
Regulation of different kinases for Alzheimer's disease therapy: progresses and perspectives
Han, M., Liao, Q., He, S., Guo, L., Lu, Z., Wang, X., Sun, W., Duan, Y. B., Lyu, W., & Li, Q. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110300
Zhang, Y.-Y., Long, X.-Y., Wang, K.-J., Tian, J., Xu, J., & Luo, X. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-026-01904-8
Liu, D., Zhuo, Y., Chen, S., Wang, Y., Chen, X., & Yao, Y. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1845934
“Our study advances rather than reiterates prior findings: Tu et al. (2010) linked DAPK1-NMDAR2B interaction to stroke but not to apoE4 or AD, while Veinbergs et al. (2002) reported apoE4-induced calcium imbalance without identifying DAPK1-NMDAR2B as a mediator.”
Peng, L., Li, Q., Li, Z., Bai, G., Tian, Y., & Zhou, S. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c11943
Self-citationZhai, C.-Z., Cao, Y., Shen, Y., Wang, Y., Liu, Z., Liu, F., Yu, J.-L., Wang, X.-X., Zhang, Z., & Xu, X. (2026) · Neuropharmacology · doi:10.1016/j.neuropharm.2026.111195
Self-citationWang, K., Zhang, W., Wang, Q., Li, G., Chen, Y., & He, Z. (2026) · Research Square · doi:10.21203/rs.3.rs-10189227/v1
Self-citationLi, B., Ming, R., Wu, Z., & Pan, S. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-03299-9
Dhurandhar, Y., Tomar, S., Bisen, V., & Namdeo, K. P. (2026) · Medical Hypotheses · doi:10.1016/j.mehy.2026.112208
Metadata
- 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
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 140
- Issue
- 2
- Pages
- 222-234
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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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