Trafficking and synaptic anchoring of ionotropic inhibitory neurotransmitter receptors.
Standard
Trafficking and synaptic anchoring of ionotropic inhibitory neurotransmitter receptors. / Kneussel, Matthias; Löbrich, Sven.
in: BIOL CELL, Jahrgang 99, Nr. 6, 6, 2007, S. 297-309.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
RIS
TY - JOUR
T1 - Trafficking and synaptic anchoring of ionotropic inhibitory neurotransmitter receptors.
AU - Kneussel, Matthias
AU - Löbrich, Sven
PY - 2007
Y1 - 2007
N2 - Neurotransmitter receptors are subject to microtubule-based transport between intracellular organelles and the neuronal plasma membrane. Receptors that arrive at plasma membrane compartments diffuse laterally within the plane of the cellular surface. To achieve immobilization at their sites of action, cytoplasmic receptor residues bind to submembrane proteins, which are coupled to the underlying cytoskeleton by multiprotein scaffolds. GABA(A)Rs (gamma-aminobutyric type A receptors) and GlyRs (glycine receptors) are the major inhibitory receptors in the central nervous system. At inhibitory postsynaptic sites, all GlyRs and the majority of GABA(A)Rs directly or indirectly couple to gephyrin, a multimeric PSD (postsynaptic density) component. In addition to cluster formations at axo-dendritic contacts, individual GABA(A)R subtypes also anchor and concentrate at extrasynaptic positions, either through association with gephyrin or direct interaction with the ERM (ezrin/radixin/moesin) family protein radixin. In addition to their role in diffusion trapping of surface receptors, scaffold components also undergo rapid exchange to/from and between postsynaptic specializations, leading to a dynamic equilibrium of receptor-scaffold complexes. Moreover, scaffold components serve as adaptor proteins that mediate specificity in intracellular transport complexes. In the present review, we discuss the dynamic delivery, stabilization and removal of inhibitory receptors at synaptic sites.
AB - Neurotransmitter receptors are subject to microtubule-based transport between intracellular organelles and the neuronal plasma membrane. Receptors that arrive at plasma membrane compartments diffuse laterally within the plane of the cellular surface. To achieve immobilization at their sites of action, cytoplasmic receptor residues bind to submembrane proteins, which are coupled to the underlying cytoskeleton by multiprotein scaffolds. GABA(A)Rs (gamma-aminobutyric type A receptors) and GlyRs (glycine receptors) are the major inhibitory receptors in the central nervous system. At inhibitory postsynaptic sites, all GlyRs and the majority of GABA(A)Rs directly or indirectly couple to gephyrin, a multimeric PSD (postsynaptic density) component. In addition to cluster formations at axo-dendritic contacts, individual GABA(A)R subtypes also anchor and concentrate at extrasynaptic positions, either through association with gephyrin or direct interaction with the ERM (ezrin/radixin/moesin) family protein radixin. In addition to their role in diffusion trapping of surface receptors, scaffold components also undergo rapid exchange to/from and between postsynaptic specializations, leading to a dynamic equilibrium of receptor-scaffold complexes. Moreover, scaffold components serve as adaptor proteins that mediate specificity in intracellular transport complexes. In the present review, we discuss the dynamic delivery, stabilization and removal of inhibitory receptors at synaptic sites.
M3 - SCORING: Zeitschriftenaufsatz
VL - 99
SP - 297
EP - 309
JO - BIOL CELL
JF - BIOL CELL
SN - 0248-4900
IS - 6
M1 - 6
ER -