CaMKII activation persistently segregates postsynaptic proteins via liquid phase separation
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Abstract
Transient information input to the brain leads to persistent changes in synaptic circuits, contributing to the formation of memory engrams. Pre- and postsynaptic structures undergo coordinated functional and structural changes during this process, but how such changes are achieved by their component molecules remains largely unknown. We found that activated CaMKII, a central player of synaptic plasticity, undergoes liquid-liquid phase separation with the NMDA-type glutamate receptor subunit GluN2B. Due to CaMKII autophosphorylation, the condensate stably persists even after Ca 2+ is removed. The selective binding of activated CaMKII with GluN2B cosegregates AMPA receptors and the synaptic adhesion molecule neuroligin into a phase-in-phase assembly. In this way, Ca 2+-induced liquid-liquid phase separation of CaMKII has the potential to act as an activity-dependent mechanism to crosslink postsynaptic proteins, which may serve as a platform for synaptic reorganization associated with synaptic plasticity.
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In the LLPS study, the CaMKII-GluN2B CTD dissipated after removal of Ca2+ unless the kinase was allowed to autophosphorylate.
“However, in the LLPS study, even after long incubation the CaMKII-GluN2B CTD dissipated after removal of Ca2+ unless the kinase was allowed to autophosphorylate, albeit slowly.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
The 'Autophosphorylation of CaMKII is required for persistence of protein condensate' section reports that CaMKII–GluN2Bc condensates dissolved after Ca²⁺ chelation when ATP was absent or CaMKII could not autophosphorylate at T286. It does not establish the claim's 'even after long incubation' qualification. Its turbidity results instead report a return to baseline within 30 seconds after chelation for the T286A mutant, rather than slow dissipation. (LLM, conf=0.86)
Experimental — accuracy not yet measuredAs long as Ca2+/CaM is present, binding and phase separation are maintained even with a phosphonull mutant of T286 (T286A) or with a kinase-dead mutant of CaMKII, although the binding of CaMKII to GluN2B is modestly enhanced by T286 phosphorylation.
“As long as Ca2+/CaM is present, binding and phase separation are maintained even with a phosphonull mutant of T286 (T286A) (78, 169, 323, 377) or with a kinase-dead mutant of CaMKII (169, 323, 378, 379), although the binding of CaMKII to GluN2B is modestly enhanced by T286 phosphorylation (378).”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
Split into 2 atoms — 1 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredSuch a CaMKII-GluN2B hub may be the driver of increased AMPAR/TARPs that is the basis for LTP expression.
“Such a CaMKII-GluN2B hub may be the driver of increased AMPAR/TARPs that is the basis for LTP expression.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
The Discussion (page unavailable) proposes a CaMKII–GluN2B condensate that may enrich AMPARs beneath transmitter-release sites, and the results use the TARP stargazin as an AMPAR proxy. The paper links this mechanism to synaptic plasticity, but does not establish an increase in AMPAR/TARP abundance or show that it is the basis of LTP expression. (LLM, conf=0.83)
Experimental — accuracy not yet measuredOur findings in HEK cells confirm prior results with cell-free assays indicating that Ca2+/CaM stimulation is sufficient for the induction of condensation but that pT286 is required for its maintenance beyond the initial stimulus.
“For CaMKII co-condensation with GluN2B, our findings in HEK cells confirm prior results with cell-free assays20,21 indicating that Ca2+/CaM stimulation is sufficient for the induction of condensation but that pT286 is required for its maintenance beyond the initial stimulus.”
From LTP expression mediated by autonomous activity of GluN2B-bound CaMKII (2024) · cites this paper as [20]
When AMPAR/TARPs and PSD-95 are added, activation of CaMKII in the presence of ATP partitions AMPAR/TARPs and NMDARs into two different phases.
“Furthermore, when AMPAR/TARPs (represented by the CTD of the auxiliary TARP subunit Stargazin) and PSD-95 are added to the system, activation of CaMKII in the presence of ATP partitions AMPAR/TARPs and NMDARs into two different phases (FIGURE 8).”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
In the LLPS study, autophosphorylation is necessary for persistence of the condensate.
“In the LLPS study, autophosphorylation is necessary for persistence of the condensate.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
A mixture of the GluN2B CTD and CaMKII undergoes liquid-liquid phase separation when Ca2+/CaM binds to CaMKII in either the absence or presence of ATP.
“The authors show that a mixture of the GluN2B CTD and CaMKII undergoes liquid-liquid phase separation (LLPS) when Ca2+/CaM binds to CaMKII in either the absence or presence of ATP.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
When the CTD of neuroligin 1 is included, it partitions with AMPAR/TARPs but not with NMDARs, reminiscent of nanocolumns in the PSD.
“Remarkably, when the CTD of neuroligin 1 is included, it partitions with the AMPAR/TARPs but not with the NMDARs, reminiscent of nanocolumns in the PSD (251–253)”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
In both LLPS and biochemical complex formation, addition of Ca2+/CaM in the absence of ATP or with the T286A mutant was sufficient for LLPS or complex formation.
“In both cases addition of Ca2+/CaM in the absence of ATP or with the T286A mutant was sufficient for the LLPS or complex formation.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
Phase separation resulting from GluN2B CTD and CaMKII mixed in the presence of Ca2+/CaM remains intact after removal of Ca2+, but only if T286 is phosphorylated.
“The phase separation resulting from GluN2B CTD and CaMKII mixed in the presence of Ca2+/CaM remains intact after the removal of Ca2+, but only if T286 is phosphorylated.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
Maintenance of segregation in the LLPS study required T286 autophosphorylation but did not require phosphorylation of any other component of the reconstituted system.
“Importantly, although the maintenance of this segregation in the LLPS study required T286 autophosphorylation, it did not require the phosphorylation of any other component of the reconstituted system.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
The Ca2+/CaM-dependent binding and phase separation (LLPS) of CaMKII to GluN2B can occur in the absence of enzymatic activity.
“It is well established that the Ca2+/CaM-dependent binding and phase separation (LLPS) of CaMKII to GluN2B can occur in the absence of enzymatic activity (169, 323, 376).”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
T286 phosphorylation plays a role in the maintenance of liquid-liquid phase separation (LLPS).
“T286 phosphorylation plays a role in the maintenance of liquid-liquid phase separation (LLPS) (323).”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
The CaMKII-GluN2B complex undergoes liquid-liquid phase separation (LLPS).
“The recent findings of Hosokawa et al. (323) show that the CaMKII-GluN2B undergoes LLPS.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
LLPS orchestrates a phase-in-phase condensation of AMPAR/TARPs, PSD-95, and neuroligin1, largely independent of phosphorylation, although T286 phosphorylation is required for the maintenance of the condensates.
“Most intriguingly, this orchestrates a phase-in-phase condensation of AMPAR/TARPs, PSD-95, and neuroligin1, largely independent of phosphorylation, although T286 phosphorylation is required for the maintenance of the condensates.”
From Synaptic memory and CaMKII (2023) · cites this paper as [323]
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“These studies can inform our investigation of possible LLPS involvement in signaling at the PSD. Condensates require proteins capable of multi-valent interactions to produce a mesh or network that concentrate proteins and drive phase separation.”
BackgroundInfluentialLTP induction by structural rather than enzymatic functions of CaMKII
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Self-citationLiquid-Liquid Phase Separation in Physiology and Pathophysiology of the Nervous System
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Self-citationIntegrated proteogenomic characterization of medullary thyroid carcinoma
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A revised view of the role of CaMKII in learning and memory
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Quantifying postsynaptic receptor dynamics: insights into synaptic function
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In vivo nanoscopic landscape of neurexin ligands underlying anterograde synapse specification
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CaMKII autophosphorylation is the only enzymatic event required for synaptic memory
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Self-citationSynaptic BMAL1 phosphorylation controls circadian hippocampal plasticity
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Half a century legacy of long-term potentiation
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Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System
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Synaptic memory survives molecular turnover
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Modulation of biomolecular phase behavior by metal ions
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Synapse-specific structural plasticity that protects and refines local circuits during LTP and LTD
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Ketamine alleviates NMDA receptor hypofunction through synaptic trapping
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Self-citationThe rheology and interfacial properties of biomolecular condensates
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Self-citationLocation, location, location: Protein kinase nanoclustering for optimised signalling output
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LTP expression mediated by autonomous activity of GluN2B-bound CaMKII
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A glutamate receptor C-tail recruits CaMKII to suppress retrograde homeostatic signaling
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Self-citationTrans-synaptic molecular context of NMDA receptor nanodomains
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Self-citationThermodynamic modulation of gephyrin condensation by inhibitory synapse components
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Molecular mechanisms of AMPAR reversible stabilization at synapses
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Multiphasic protein condensation governed by shape and valency
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Self-citationThe synaptic vesicle cluster as a controller of pre‐ and postsynaptic structure and function
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Phase Separation–Mediated Compartmentalization Underlies Synapse Formation and Plasticity
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Self-citationMulti-dimensional condensation of intracellular biomolecules
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Transient, nano-scale, liquid-like molecular assemblies coming of age
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Postsynaptic protein assembly in three and two dimensions studied by mesoscopic simulations
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Self-citationAlteration of synaptic protein composition during developmental synapse maturation
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Tuning synapse strength by nanocolumn plasticity
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Inhibitory postsynaptic density from the lens of phase separation
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Phase separation in the multi-compartment organization of synapses
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Self-citationBasak, S., Saikia, N., Kwun, D., Choi, U. B., Ding, F., & Bowen, M. E. (2022) · Biomolecules · doi:10.3390/biom13010004 · Cited by 6 · see citing works
Two-dimensional interfacial diffusion model of inhibitory synaptic receptor dynamics
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CaMKII autophosphorylation but not downstream kinase activity is required for synaptic memoryPreprint
Chen, X., Cai, Q., Zhou, J., Pleasure, S. J., Schulman, H., Zhang, M., & Nicoll, R. A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.25.554912 · Cited by 7 · see citing works
Self-citationAPOE4 triggers dysregulated synaptic vesicle release by disrupting SNARE complex assembly
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Orchestrating synaptic strength by neuroligin-confined nanoscale organization
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Regulation of Presynaptic Release Machinery by Cell Adhesion Molecules
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Self-citationCa2+/calmodulin signaling in organismal aging and cellular senescence: Impact on human diseases
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AMPA and GABAA receptor nanodomains assemble in the absence of synaptic neurotransmitter release
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PICK1 links KIBRA and AMPA receptor subunit GluA2 in coiled-coil-driven supramolecular complexes
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Generation of Conformation‐Specific Monoclonal Antibodies for Integral Membrane Proteins
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The Janus face of CaMKII: from memory consolidation to neurotoxic switch in Alzheimer’s disease
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Environmental signals driving liquid-liquid phase separation – a molecular memory in plants?
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Scales of Postsynaptic Nanostructure: Molecules, Nanoclusters, and Nanodomains
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Long-term potentiation in the brain: a synaptic memory mechanism
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nArgBP2 together with GKAP and SHANK3 forms a dynamic layered structure
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AMPA receptors in synaptic plasticity and learning and memory
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Condensed matter biology: from phase separation to percolated network
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CaMKII nucleates an osmotic protein supercomplex to induce cellular bleb expansion
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Liquid–liquid phase separation in neural development
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On independency of functional and morphological synapse plasticity
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CaMKII as a Multimodal Signalling Hub in Neural Connectivity and Vulnerability
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- Authors
- Hosokawa, T., Liu, P.-W., Cai, Q., Ferreira, J. S., Levet, F., Butler, C., Sibarita, J.-B., Choquet, D., Groc, L., Hosy, E., Zhang, M., & Hayashi, Y.
- Affiliations
- Kyoto University (JP)
- Hong Kong University of Science and Technology (HK)
- Université de Bordeaux (FR)
- Corresponding author
- Zhang, Mingjie
- Hayashi, Yasunori
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2021-04-29
- Volume
- 24
- Issue
- 6
- Pages
- 777-785
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- OpenAlex
- W3157311560
- Cited by
- 146
- References
- 73
- Citations by year
- 2026: 26 · 2025: 26 · 2024: 33 · 2023: 28 · 2022: 23 · 2021: 10
- FWCI
- 10.86
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Nature Neuroscience (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- Simons Foundation (510178)
- Naito Foundation
- Takeda Science Foundation
- Novartis Foundation
- Japan Foundation for Applied Enzymology
- Uehara Memorial Foundation
- Agence Nationale de la Recherche
- Ministry of Education, Culture, Sports, Science and Technology (17K14947, 18H04733, 22110006, 18H05434, 20240032, 18KK0421)
- Centre National de la Recherche Scientifique
- Research Foundation for Opto-Science and Technology
- National Institutes of Health (16H01292)
- Japan Society for the Promotion of Science (20240032, 16H01292, 20K21462, 22110006, 18H05428, 18H05434, 18H04733, 18KK0421, 22KF0163, 19K06885, 17K14947)
- RIKEN (22110006, 20240032, 18H04733, 18H05434)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- CaMKII, liquid-liquid phase separation, GluN2B, NMDA receptor, AMPA receptors, neuroligins, postsynaptic proteins, synaptic plasticity, calcium signaling, autophosphorylation, memory engrams, synaptic transmission
- MeSH terms
- Amino Acid Sequence, Animals, Enzyme Activation, Female, Male, Membrane Proteins, Receptors, N-Methyl-D-Aspartate, Rats, Sprague-Dawley, Receptors, AMPA, Mice, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Liquid-Liquid Extraction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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