GluN2B influences the progression of status epilepticus by modulating calcium ion homeostasis through its interaction with CaMKIIα
The reduction in CaMKIIα phosphorylation levels depends on the NMDAR pathway. When GluN2B binds to CaMKIIα, it may occupy the autophosphorylation site of CaMKIIα (T286 binding site), thereby affecting its autophosphorylation. This results in decreased phosphorylation levels, disruption of NMDAR-dependent calcium homeostasis, and alteration of the excitation/inhibition balance.
Authors
- Chaoning Liu (ORCID: https://orcid.org/0000-0003-2292-2578)
- Donghua Zou (ORCID: https://orcid.org/0000-0002-3891-9472)
- Yuling Lu (ORCID: https://orcid.org/0000-0002-3847-3255)
- Shun Zheng (ORCID: https://orcid.org/0009-0004-3643-895X)
- Lei Wei (ORCID: https://orcid.org/0000-0001-5140-0504)
- Youshi Meng
- Yuan Wu (ORCID: https://orcid.org/0000-0001-5016-1660)
- Lin Zhang (ORCID: https://orcid.org/0009-0001-0450-2361)
Institutions
- Guangxi Medical University (CN)
- First Affiliated Hospital of GuangXi Medical University (CN)
Publication Details
- Journal
- Frontiers in Pharmacology
- Published
- 2025-04-22
- DOI
- https://doi.org/10.3389/fphar.2025.1550879
- Primary Topic
- Neuroscience and Neuropharmacology Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Guangxi Key Research and Development Program