Cellular transport and membrane dynamics of the glycine receptor.

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Cellular transport and membrane dynamics of the glycine receptor. / Dumoulin, Andrea; Triller, Antoine; Kneussel, Matthias.

In: FRONT MOL NEUROSCI, Vol. 2, 2010, p. 28.

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@article{f904fb618a154a73955e5b2f4d4adcd9,
title = "Cellular transport and membrane dynamics of the glycine receptor.",
abstract = "Regulation of synaptic transmission is essential to tune individual-to-network neuronal activity. One way to modulate synaptic strength is to regulate neurotransmitter receptor numbers at postsynaptic sites. This can be achieved either through plasma membrane insertion of receptors derived from intracellular vesicle pools, a process depending on active cytoskeleton transport, or through surface membrane removal via endocytosis. In parallel, lateral diffusion events along the plasma membrane allow the exchange of receptor molecules between synaptic and extrasynaptic compartments, contributing to synaptic strength regulation. In recent years, results obtained from several groups studying glycine receptor (GlyR) trafficking and dynamics shed light on the regulation of synaptic GlyR density. Here, we review (i) proteins and mechanisms involved in GlyR cytoskeletal transport, (ii) the diffusion dynamics of GlyR and of its scaffolding protein gephyrin that control receptor numbers, and its relationship with synaptic plasticity, and (iii) adaptative changes in GlyR diffusion in response to global activity modifications, as a homeostatic mechanism.",
author = "Andrea Dumoulin and Antoine Triller and Matthias Kneussel",
year = "2010",
doi = "10.3389/neuro.02.028.2009",
language = "Deutsch",
volume = "2",
pages = "28",
journal = "FRONT MOL NEUROSCI",
issn = "1662-5099",
publisher = "Frontiers Research Foundation",

}

RIS

TY - JOUR

T1 - Cellular transport and membrane dynamics of the glycine receptor.

AU - Dumoulin, Andrea

AU - Triller, Antoine

AU - Kneussel, Matthias

PY - 2010

Y1 - 2010

N2 - Regulation of synaptic transmission is essential to tune individual-to-network neuronal activity. One way to modulate synaptic strength is to regulate neurotransmitter receptor numbers at postsynaptic sites. This can be achieved either through plasma membrane insertion of receptors derived from intracellular vesicle pools, a process depending on active cytoskeleton transport, or through surface membrane removal via endocytosis. In parallel, lateral diffusion events along the plasma membrane allow the exchange of receptor molecules between synaptic and extrasynaptic compartments, contributing to synaptic strength regulation. In recent years, results obtained from several groups studying glycine receptor (GlyR) trafficking and dynamics shed light on the regulation of synaptic GlyR density. Here, we review (i) proteins and mechanisms involved in GlyR cytoskeletal transport, (ii) the diffusion dynamics of GlyR and of its scaffolding protein gephyrin that control receptor numbers, and its relationship with synaptic plasticity, and (iii) adaptative changes in GlyR diffusion in response to global activity modifications, as a homeostatic mechanism.

AB - Regulation of synaptic transmission is essential to tune individual-to-network neuronal activity. One way to modulate synaptic strength is to regulate neurotransmitter receptor numbers at postsynaptic sites. This can be achieved either through plasma membrane insertion of receptors derived from intracellular vesicle pools, a process depending on active cytoskeleton transport, or through surface membrane removal via endocytosis. In parallel, lateral diffusion events along the plasma membrane allow the exchange of receptor molecules between synaptic and extrasynaptic compartments, contributing to synaptic strength regulation. In recent years, results obtained from several groups studying glycine receptor (GlyR) trafficking and dynamics shed light on the regulation of synaptic GlyR density. Here, we review (i) proteins and mechanisms involved in GlyR cytoskeletal transport, (ii) the diffusion dynamics of GlyR and of its scaffolding protein gephyrin that control receptor numbers, and its relationship with synaptic plasticity, and (iii) adaptative changes in GlyR diffusion in response to global activity modifications, as a homeostatic mechanism.

U2 - 10.3389/neuro.02.028.2009

DO - 10.3389/neuro.02.028.2009

M3 - SCORING: Zeitschriftenaufsatz

VL - 2

SP - 28

JO - FRONT MOL NEUROSCI

JF - FRONT MOL NEUROSCI

SN - 1662-5099

ER -