TY - JOUR
T1 - Differential distribution of glycine receptor subtypes at the rat calyx of held synapse
AU - Hruskova, Bohdana
AU - Trojanova, Johana
AU - Kulik, Akos
AU - Kralikova, Michaela
AU - Pysanenko, Kateryna
AU - Bures, Zbynek
AU - Syka, Josef
AU - Trussell, Laurence O.
AU - Turecek, Rostislav
PY - 2012/11/21
Y1 - 2012/11/21
N2 - The properties of glycine receptors (GlyRs) depend upon their subunit composition. While the prevalent adult forms of GlyRs are heteromers, previous reports suggested functional α homomeric receptors in mature nervous tissues. Here we show two functionally different GlyRs populations in the rat medial nucleus of trapezoid body (MNTB). Postsynaptic receptors formed α1/β-containing clusters on somatodendritic domains of MNTB principal neurons, colocalizing with glycinergic nerve endings to mediate fast, phasic IPSCs. In contrast, presynaptic receptors on glutamatergic calyx of Held terminals were composed of dispersed, homomeric α1 receptors. Interestingly, the parent cell bodies of the calyces of Held, the globular bushy cells of the cochlear nucleus, expressed somatodendritic receptors (α1/β heteromers) and showed similar clustering and pharmacological profile as GlyRs on MNTB principal cells. These results suggest that specific targeting of GlyR β-subunit produces segregation of GlyR subtypes involved in two different mechanisms of modulation of synaptic strength.
AB - The properties of glycine receptors (GlyRs) depend upon their subunit composition. While the prevalent adult forms of GlyRs are heteromers, previous reports suggested functional α homomeric receptors in mature nervous tissues. Here we show two functionally different GlyRs populations in the rat medial nucleus of trapezoid body (MNTB). Postsynaptic receptors formed α1/β-containing clusters on somatodendritic domains of MNTB principal neurons, colocalizing with glycinergic nerve endings to mediate fast, phasic IPSCs. In contrast, presynaptic receptors on glutamatergic calyx of Held terminals were composed of dispersed, homomeric α1 receptors. Interestingly, the parent cell bodies of the calyces of Held, the globular bushy cells of the cochlear nucleus, expressed somatodendritic receptors (α1/β heteromers) and showed similar clustering and pharmacological profile as GlyRs on MNTB principal cells. These results suggest that specific targeting of GlyR β-subunit produces segregation of GlyR subtypes involved in two different mechanisms of modulation of synaptic strength.
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U2 - 10.1523/JNEUROSCI.1547-12.2012
DO - 10.1523/JNEUROSCI.1547-12.2012
M3 - Article
C2 - 23175852
AN - SCOPUS:84870045464
SN - 0270-6474
VL - 32
SP - 17012
EP - 17024
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 47
ER -