ArticleNature communications2026
Dynamic recruitment of CaMKII into SHANK3 phase-separated condensates tunes postsynaptic density remodeling during long-term potentiation.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Biomolecular condensation of cMLCK enables myosin motor phosphorylation in the heart.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activity-dependent postsynaptic density (PSD) remodeling orchestrates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) trafficking during long-term potentiation (LTP), yet the underlying mechanisms remain poorly understood. Here, we demonstrate that SHANK3 critically mediates the rapid recruitment of Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) to PSD and the ensuing PSD remodeling through liquid‒liquid phase separation (LLPS). We found that deletion of the large intrinsically disordered region (IDR) of SHANK3 impairs its LLPS and clustering at dendritic spines of mouse hippocampal neurons, leading to reduction in PSD size and AMPAR expression. Activation of photoactivatable CaMKII promotes its rapid recruitment to SHANK3 condensates, facilitating condensate fusion and PSD remodeling. A human autism-related SHANK3 mutation (InsG3680) truncates part of the large IDR, disrupts SHANK3 LLPS, and causes deficits in PSD remodeling and AMPAR recruitment. Overall, we propose that activity-dependent modulation of SHANK3 condensate dynamics via CaMKII recruitment is a mechanism underlying PSD reorganization during LTP.
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.