ArticleCommunications biology2025
SNX6-mediated subunit-specific secretory trafficking of AMPA receptors regulates synaptic function and plasticity.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
The AMPA-type glutamate receptors (AMPARs) mediate the majority of fast excitatory synaptic transmission in the brain and are central to synaptic plasticity in excitatory neurons. Functional AMPARs are tetramers composed of different combinations of the channel-forming GluA1-GluA4 subunits, with GluA2 critically influencing receptor biophysics and trafficking. However, the mechanisms governing AMPAR subunit-specific trafficking and assembly in resting and activated neurons remain incompletely understood. Using hippocampal neurons and conditional knockout mice, we demonstrate that sorting nexin 6 (SNX6), a membrane trafficking regulator, selectively mediates sorting of newly synthesized GluA2 into the post-Golgi secretory pathway before its assembly with GluA1, a process essential for AMPAR delivery to the plasma membrane. Loss of SNX6 diverts GluA2 to lysosomal degradation, leading to decreases in constitutive and activity-dependent surface expression of AMPARs, impairment of AMPAR-mediated synaptic transmission and the NMDA-type glutamate receptor (NMDAR)-dependent long-term potentiation, and deficits in learning and memory. Collectively, our findings reveal a novel, subunit-specific mechanism for AMPAR biogenesis and trafficking, and underscore the importance of regulatory steps within the biosynthetic secretory pathway in synaptic receptor delivery.
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.