Correction: A model for regulation by SynGAP-α1 of binding of synaptic proteins to PDZ-domain 'Slots' in the postsynaptic density
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Phosphorylation-induced dissociation of SynGAP from PSD-95 is proposed to free PDZ domains, creating slots for AMPARs/TARPs.
“The phosphorylation-induced dissociation of SynGAP from the PSD-95 is proposed to free up PDZ domains, creating slots for AMPARs/TARPs (302).”
From Synaptic memory and CaMKII (2023) · cites this paper as [302]
CaMKII phosphorylates SynGAP and decreases its binding to PSD-95.
“CaMKII phosphorylates SynGAP and decreases its binding to PSD-95 (302, 304).”
From Synaptic memory and CaMKII (2023) · cites this paper as [302]
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Nicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
- Authors
- Walkup, W. G., Mastro, T. L., Schenker, L. T., Vielmetter, J., Hu, R., Iancu, A., Reghunathan, M., Bannon, B. D., & Kennedy, M. B.
- Corresponding author
- Kennedy, Mary B
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2016-10-19
- Volume
- 5
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC5070946
- OpenAlex
- W4234982986
- Cited by
- 14
- References
- 0
- Citations by year
- 2025: 2 · 2024: 3 · 2023: 6 · 2022: 1 · 2021: 1 · 2020: 1
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- SynGAP, PDZ domain, postsynaptic density, synaptic proteins, protein binding, synaptic regulation
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