Editing AMPA receptor (section)

==== Biophysics of AMPA receptor trafficking ====
The movement of AMPA receptors within the neuronal membrane is commonly modeled as [[Brownian diffusion]], reflecting their lateral mobility across the lipid bilayer.  However, at synaptic sites— particularly the [[postsynaptic density]] (PSD)—this motion is modulated by retention forces that can transiently stabilize receptors.<ref name=":3">{{Cite journal |vauthors=Heine M, Groc L, Frischknecht R, Béïque JC, Lounis B, Rumbaugh G, Huganir RL, Cognet L, Choquet D |date=April 2008 |title=Surface Mobility of Postsynaptic AMPARs Tunes Synaptic Transmission |journal=Science |volume=320 |issue=5873 |pages=201–205 |bibcode=2008Sci...320..201H |doi=10.1126/science.1152089 |pmc=2715948 |pmid=18403705}}</ref><ref name=":4">{{Cite journal |last1=He |first1=Shao-Qiu |last2=Zhang |first2=Zhen-Ning |last3=Guan |first3=Ji-Song |last4=Liu |first4=Hong-Rui |last5=Zhao |first5=Bo |last6=Wang |first6=Hai-Bo |last7=Li |first7=Qian |last8=Yang |first8=Hong |last9=Luo |first9=Jie |last10=Li |first10=Zi-Yan |last11=Wang |first11=Qiong |last12=Lu |first12=Ying-Jin |last13=Bao |first13=Lan |last14=Zhang |first14=Xu |date=January 2011 |title=Facilitation of μ-Opioid Receptor Activity by Preventing δ-Opioid Receptor-Mediated Codegradation |url=https://linkinghub.elsevier.com/retrieve/pii/S0896627310009864 |journal=Neuron |language=en |volume=69 |issue=1 |pages=120–131 |doi=10.1016/j.neuron.2010.12.001|pmid=21220103 }}</ref><ref>{{Cite journal |vauthors=Hoze N, Nair D, Hosy E, Holcman D |date=October 2012 |title=Heterogeneity of AMPA receptor trafficking and molecular interactions revealed by superresolution analysis of live cell imaging |journal=Proceedings of the National Academy of Sciences |volume=109 |issue=42 |pages=17052–17057 |doi=10.1073/pnas.1204589109 |pmid=23035245 |pmc=3479500 |bibcode=2012PNAS..10917052H |doi-access=free}}</ref> These forces do not completely immobilize AMPARs but instead permit a dynamic exchange with receptors in the perisynaptic domain.<ref name=":3" /><ref name=":4" /> 

The molecular basis for this stabilization is believed to involve nanodomain organization within the PSD, including anchoring interactions with scaffolding proteins such as PSD-95 and transmembrane AMPA receptor regulatory proteins (TARPs).<ref name=":5">{{Cite journal |last1=Liu |first1=Zhikai |last2=Kimura |first2=Yukiko |last3=Higashijima |first3=Shin-ichi |last4=Hildebrand |first4=David G.C. |last5=Morgan |first5=Joshua L. |last6=Bagnall |first6=Martha W. |date=November 2020 |title=Central Vestibular Tuning Arises from Patterned Convergence of Otolith Afferents |journal=Neuron |language=en |volume=108 |issue=4 |pages=748–762.e4 |doi=10.1016/j.neuron.2020.08.019 |pmc=7704800 |pmid=32937099}}</ref><ref name=":6">{{Cite journal |last1=Anastasi |first1=Sergio |last2=Zhu |first2=Su-Jie |last3=Ballarò |first3=Costanza |last4=Manca |first4=Sonia |last5=Lamberti |first5=Dante |last6=Wang |first6=Li-Jun |last7=Alemà |first7=Stefano |last8=Yun |first8=Cai-Hong |last9=Segatto |first9=Oreste |date=May 2016 |title=Lack of Evidence that CYTH2/ARNO Functions as a Direct Intracellular EGFR Activator |url=https://linkinghub.elsevier.com/retrieve/pii/S0092867416305578 |journal=Cell |language=en |volume=165 |issue=5 |pages=1031–1034 |doi=10.1016/j.cell.2016.05.009|pmid=27203102 }}</ref> Recent evidence suggests that this compartmentalization may arise through liquid-liquid [[phase separation]] (LLPS), a biophysical process by which biomolecular condensates form via weak, multivalent interactions.  LLPS may contribute to the formation of synaptic nanodomains that selectively retain or enrich AMPARs at functional sites within the PSD.<ref name=":5" /><ref name=":6" />