Activated radixin is essential for GABAA receptor alpha5 subunit anchoring at the actin cytoskeleton.
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Activated radixin is essential for GABAA receptor alpha5 subunit anchoring at the actin cytoskeleton. / Loebrich, Sven; Bähring, Robert; Katsuno, Tatsuya; Tsukita, Sachiko; Kneussel, Matthias.
In: EMBO J, Vol. 25, No. 5, 5, 2006, p. 987-999.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Activated radixin is essential for GABAA receptor alpha5 subunit anchoring at the actin cytoskeleton.
AU - Loebrich, Sven
AU - Bähring, Robert
AU - Katsuno, Tatsuya
AU - Tsukita, Sachiko
AU - Kneussel, Matthias
PY - 2006
Y1 - 2006
N2 - Neurotransmitter receptor clustering is thought to represent a critical parameter for neuronal transmission. Little is known about the mechanisms that anchor and concentrate inhibitory neurotransmitter receptors in neurons. GABAA receptor (GABAAR) alpha5 subunits mainly locate at extrasynaptic sites and are thought to mediate tonic inhibition. Notably, similar as synaptic GABAARs, these receptor subtypes also appear in cluster formations at neuronal surface membranes and are of particular interest in cognitive processing. GABAAR alpha5 mutation or depletion facilitates trace fear conditioning or improves spatial learning in mice, respectively. Here, we identified the actin-binding protein radixin, a member of the ERM family, as the first directly interacting molecule that anchors GABAARs at cytoskeletal elements. Intramolecular activation of radixin is a functional prerequisite for GABAAR alpha5 subunit binding and both depletion of radixin expression as well as replacement of the radixin F-actin binding motif interferes with GABAAR alpha5 cluster formation. Our data suggest radixin to represent a critical factor in receptor localization and/or downstream signaling.
AB - Neurotransmitter receptor clustering is thought to represent a critical parameter for neuronal transmission. Little is known about the mechanisms that anchor and concentrate inhibitory neurotransmitter receptors in neurons. GABAA receptor (GABAAR) alpha5 subunits mainly locate at extrasynaptic sites and are thought to mediate tonic inhibition. Notably, similar as synaptic GABAARs, these receptor subtypes also appear in cluster formations at neuronal surface membranes and are of particular interest in cognitive processing. GABAAR alpha5 mutation or depletion facilitates trace fear conditioning or improves spatial learning in mice, respectively. Here, we identified the actin-binding protein radixin, a member of the ERM family, as the first directly interacting molecule that anchors GABAARs at cytoskeletal elements. Intramolecular activation of radixin is a functional prerequisite for GABAAR alpha5 subunit binding and both depletion of radixin expression as well as replacement of the radixin F-actin binding motif interferes with GABAAR alpha5 cluster formation. Our data suggest radixin to represent a critical factor in receptor localization and/or downstream signaling.
M3 - SCORING: Zeitschriftenaufsatz
VL - 25
SP - 987
EP - 999
JO - EMBO J
JF - EMBO J
SN - 0261-4189
IS - 5
M1 - 5
ER -
