Formation and Stability of Synaptic Receptor Domains

Haselwandter, Christoph A.; Calamai, Martino; Kardar, Mehran; Triller, Antoine; Silveira, Rava Azeredo da

doi:10.1103/physrevlett.106.238104

Cited by 43 publications

(155 citation statements)

References 32 publications

(85 reference statements)

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“…In particular, single non-neural (fibroblast) cells were transfected with neuronal receptor and scaffold molecules [14,26], allowing for the rapid diffusion of receptors [14,27,28] observed in neurons [8][9][10] as well as for interactions between receptors and scaffolds. If receptor and scaffold molecules were both present, receptor-scaffold domains (RSDs) formed spontaneously [14,[29][30][31][32][33][34][35][36]. Furthermore, RSDs were observed to be stable once they reached a characteristic size comparable to that of synaptic domains in neurons [14,26,29,37].…”

Section: Introductionmentioning

confidence: 99%

“…If receptor and scaffold molecules were both present, receptor-scaffold domains (RSDs) formed spontaneously [14,[29][30][31][32][33][34][35][36]. Furthermore, RSDs were observed to be stable once they reached a characteristic size comparable to that of synaptic domains in neurons [14,26,29,37]. If only receptors but no scaffolds were transfected, receptor domains did not emerge, apart from possible occurrences of transient microdomains [26,27].…”

Section: Introductionmentioning

confidence: 99%

“…If only scaffolds but no receptors were transfected, large intracellular blobs of scaffolds were observed, but no association with the cell membrane was detected [26,38]. Collectively, these observations suggest [29] that receptor-scaffold interactions, together with the diffusion properties of each molecular species at the membrane, are sufficient for the formation, stability, and characteristic size of synaptic receptor domains. In particular, the presence of a presynaptic terminal is not essential for the occurrence of stable RSDs.…”

Section: Introductionmentioning

confidence: 99%

“…In this article, we build on the above experimental observations and our earlier theoretical work [29] to develop a comprehensive model of synaptic domains in terms of the underlying reaction and diffusion properties of receptor and scaffold molecules. Our article is organized as follows.…”

Section: Introductionmentioning

confidence: 99%

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Self-assembly and plasticity of synaptic domains through a reaction-diffusion mechanism

et al. 2015

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Signal transmission across chemical synapses relies crucially on neurotransmitter receptor molecules, concentrated in postsynaptic membrane domains along with scaffold and other postsynaptic molecules. The strength of the transmitted signal depends on the number of receptor molecules in postsynaptic domains, and activity-induced variation in the receptor number is one of the mechanisms of postsynaptic plasticity. Recent experiments have demonstrated that the reaction and diffusion properties of receptors and scaffolds at the membrane, alone, yield spontaneous formation of receptor-scaffold domains of the stable characteristic size observed in neurons. On the basis of these experiments we develop a model describing synaptic receptor domains in terms of the underlying reaction-diffusion processes. Our model predicts that the spontaneous formation of receptor-scaffold domains of the stable characteristic size observed in experiments depends on a few key reactions between receptors and scaffolds. Furthermore, our model suggests novel mechanisms for the alignment of preand postsynaptic domains and for short-term postsynaptic plasticity in receptor number. We predict that synaptic receptor domains localize in membrane regions with an increased receptor diffusion coefficient or a decreased scaffold diffusion coefficient. Similarly, we find that activity-dependent increases or decreases in receptor or scaffold diffusion yield a transient increase in the number of receptor molecules concentrated in postsynaptic domains. Thus, the proposed reaction-diffusion model puts forth a coherent set of biophysical mechanisms for the formation, stability, and plasticity of molecular domains on the postsynaptic membrane.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Self-assembly and plasticity of synaptic domains through a reaction-diffusion mechanism

et al. 2015

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“…De fait, un modèle a été proposé pour rendre compte de la régulation des densités locales de ces molécules dans des états de quasi-équilibre [6]. La formation et la stabilité des domaines synaptiques peuvent alors être modélisées via une instabilité de Turing en termes de réaction-diffusion [7]. Les cinétiques moléculaires doivent maintenant être réconciliées avec les phénomènes biologiques.…”

Section: éDitorialunclassified

Imagerie moléculaire : vers une chimiein cellulo

Triller

2011

Med Sci (Paris)

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Glycine Receptors

Breitinger

2014

Encyclopedia of Life Sciences

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Absract The inhibitory glycine receptor is a ligand‐gated chloride channel of the cys‐loop receptor family. As a chloride‐selective channel, it mediates rapid synaptic inhibition in mammalian spinal cord, brainstem, higher brain centres and nonneuronal tissues. In recent years, our understanding of glycine receptors has steadily grown, adding considerable depth to our knowledge of receptor function, structure, cellular trafficking and tissue distribution. Furthermore, new roles for glycinergic transmission in higher brain function have been uncovered. Glycine receptors should no longer be considered only as mediators of spinal reflexes, but were also found to play an important role in the modulation of higher brain function, including vision, hearing and pain signalling. The identification of novel agonists and modulators underlines the relevance of the inhibitory glycine receptor as a therapeutic target. This review extends a previous article of this series and highlights key developments in glycine receptor research over the past 2–3 years. Key Concepts: Glycine receptors are key mediators of rapid synaptic inhibition in mammalian spinal cord and higher brain centres. Glycine receptors are members of the cys‐loop family of ligand‐gated ion channel receptors. Glycinergic signalling is involved in motor control, pain signalling, vision, hearing and other brain functions. Mutations in glycine receptor genes underlie human hyperekplexia and related myoclonic diseases. New modulators of glycine receptor function are rare and of considerable medicinal interest.

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Formation and Stability of Synaptic Receptor Domains

Cited by 43 publications

References 32 publications

Self-assembly and plasticity of synaptic domains through a reaction-diffusion mechanism

Self-assembly and plasticity of synaptic domains through a reaction-diffusion mechanism

Imagerie moléculaire : vers une chimiein cellulo

Glycine Receptors

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