Characterization of glutamate receptor interacting protein-immunopositive neurons in cerebellum and cerebral cortex of the albino rat

Burette, A; Wyszynski, Michael; Valtschanoff, Juli G.; Sheng, Morgan; Weinberg, Richard J.

doi:10.1002/(sici)1096-9861(19990906)411:4<601::aid-cne6>3.0.co;2-3

Cited by 38 publications

(14 citation statements)

References 61 publications

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“…4C), similar to what has been reported in principal cells (Cummings et al 1996). Second, AMPA receptors lacking GluR2 might associate with specific synaptic scaffolding proteins that promote cycling of AMPA receptors to the interneuron plasma membrane (Braithwaite et al 2002;Burette et al 1999Burette et al , 2001). Likewise, GluR2-deficient synapses onto interneurons might possess uniquely specialized synaptic domains (Goldberg et al 2003), allowing a wide range of plasticity either mediated by AMPA receptors or by AMPA and NMDA receptors.…”

Section: Discussionsupporting

confidence: 55%

Voltage-Controlled Plasticity at GluR2-Deficient Synapses Onto Hippocampal Interneurons

Laezza

Dingledine

2004

Journal of Neurophysiology

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Laezza, Fernanda and Raymond Dingledine. Voltage-controlled plasticity at GluR2-deficient synapses onto hippocampal interneurons. J Neurophysiol 92: 3575-3581, 2004; doi:10.1152/jn.00425.2004. High-frequency stimulation of pyramidal cell inputs to developing (P9-12) hippocampal stratum radiatum interneurons expressing GluR2-lacking, Ca 2ϩ -permeable AMPA receptors produces longterm depression of synaptic transmission, if N-methyl-D-aspartate (NMDA) receptors are blocked. Here we show that these same synapses display a remarkably versatile signal integration if postsynaptic NMDA receptors are activated. At synapses expressing GluR2-deficient AMPA receptors, tetanic stimulation that activates NMDA receptors triggered long-term potentiation or depression (LTP or LTD) depending on membrane potential. LTP was elicited at most synapses when the interneuron was held at -30 mV during the stimulus train but was typically prevented by postsynaptic hyperpolarization to -70 mV, by strong depolarization to 0 mV, by D-2-amino-5-phosphonovaleric acid, or by postsynaptic injection of the Ca 2ϩ chelator bis-(o-aminophenoxy)-N,N,NЈ,NЈ-tetraacetic acid. At synapses with predominantly GluR2-containing AMPA receptors, repetitive stimulation did not change synaptic strength regardless of whether NMDA receptors were activated. The interactions among GluR2 expression, NMDA receptor expression, and membrane potential thus confer on hippocampal interneurons a distinctive means for differential decoding of high-frequency inputs, resulting in enhanced or depressed transmission depending on the functional state of the interneuron. I N T R O D U C T I O NThe expression of distinct synaptic receptors and voltagegated ion channels on a heterogeneous population of interneurons underlies their different integrative roles in the hippocampal circuit (Jonas et al. 2004). Long-term potentiation (LTP) and long-term depression (LTD) of excitatory synaptic strength are activity-dependent forms of synaptic plasticity triggered by Ca 2ϩ entry through postsynaptic N-methyl-D-aspartate (NMDA) receptors (Bliss and Collingridge 1993). High-frequency afferent stimulation can depress excitatory transmission to hippocampal GABAergic interneurons (Laezza et al. 1999; McBain 2002, 2004;Maccaferri et al. 1998;McMahon and Kauer 1997). An NMDA receptor-independent LTD mechanism involves Ca 2ϩ entry through postsynaptic Ca 2ϩ -permeable AMPA receptors (Laezza et al. 1999; McBain 2002, 2004) and, in stratum radiatum interneurons, activation of presynaptic mGluR7 receptors (Laezza et al. 1999). High-frequency stimulation can also potentiate synaptic inputs to interneurons via an mGluR1-dependent mechanism (Perez et al. 2001) High-frequency stimulation of pyramidal cell afferents to s. radiatum interneurons induces LTD at GluR2-deficient, but not GluR2-replete, synapses (Laezza et al. 1999). LTD occurs in the presence of NMDA receptor antagonists and is triggered by Ca 2ϩ entry through AMPA receptors. Type II EPSCs are therefore both heterogeneous in terms of NMDA re...

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Section: Discussionsupporting

confidence: 55%

Voltage-Controlled Plasticity at GluR2-Deficient Synapses Onto Hippocampal Interneurons

Laezza

Dingledine

2004

Journal of Neurophysiology

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“…Tyramide signal amplification (TSA) was used for doubleimmunofluorescent staining (Shindler and Roth, 1996;Burette et al, 1999). After overnight incubation with the first primary antibody, rabbit anti-NR1 (1:10,000; Upstate Biotechnology), sections were reacted for 2 hr at room temperature with biotinylated secondary antibody (1:400; Jackson ImmunoResearch) followed by incubation with Streptavidinperoxidase for 1 hr.…”

Section: Methodsmentioning

confidence: 99%

Group I Metabotropic Glutamate Receptor NMDA Receptor Coupling and Signaling Cascade Mediate Spinal Dorsal Horn NMDA Receptor 2B Tyrosine Phosphorylation Associated with Inflammatory Hyperalgesia

Guo¹,

Feng²,

Zou³

et al. 2004

J. Neurosci.

155

133

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“…Immunoreactivity was then visualized by donkey anti-rabbit conjugated to fluorescein isothiocyanate (FITC; Jackson ImmunoResearch). Because Pyk2, SAP102, and NR2A/B antibodies were raised in rabbit, tyramide signal amplification (TSA) was used for one of them, and subsequent conventional fluorescent staining was used for one of the other antibodies for double-labeling (72)(73)(74). After preincubation in 10% normal donkey serum, sections were incubated with Pyk2 antiserum at a dilution not recognized by a conventional fluorochrome-conjugated secondary antibody (1:20,000) and then reacted with biotinylated secondary antibody.…”

Section: Methodsmentioning

confidence: 99%

Interaction of the Tyrosine Kinase Pyk2 with the N-Methyl-d-aspartate Receptor Complex via the Src Homology 3 Domains of PSD-95 and SAP102

Seabold

Burette

Lim

et al. 2003

Journal of Biological Chemistry

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At low stimulus frequency, synaptic transmission depends largely upon ␣-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) 1 -type glutamate receptors (1, 2). High frequency stimulation promotes Ca 2ϩ influx through N-methyl-D-aspartate (NMDA) receptors, thereby inducing long term potentiation (LTP) (1,3,4). LTP is a lasting increase in synaptic transmission that may underlie learning and memory (5, 6). NMDA receptors likely consist of one or two NR1 and two or three NR2 subunits; each subunit has an extracellular N terminus and an intracellular C terminus (7-10). The very C termini of NR2 subunits interact with the first two PDZ domains of PSD-95/SAP90 and the related proteins SAP102 and PSD-93/chapsyn110. PSD-95 and its homologs (SAP102, PSD-93, and SAP97) are scaffolding proteins consisting of three PDZ domains, one SH3 domain, and one GK domain. PSD-95, PSD-93, and SAP102 are thought to be involved in clustering glutamate receptors together with other proteins at postsynaptic sites (11-15). SAP97 interacts with the AMPA receptor subunit GluR1 (16 -18). SAP97 colocalizes with GluR1, but not GluR2/3, at postsynaptic sites (17). This interaction may already occur early in the secretory pathway and may be involved in trafficking or targeting of AMPA receptors (19).SH3 and GK domains of PSD-95 and its homologs form intramolecular and, to some degree, intermolecular interactions (20 -24). A point mutation in the Drosophila protein Dlg (a homolog of PSD-95) results in the substitution of a conserved leucine in the SH3 domain to a proline; this mutation leads to the loss of septate junction formation and overproliferation of the imaginal disc (25). Replacing the homologous leucine (Leu-460) with a proline in the SH3 domain of PSD-95 inhibits the interaction of the mutant SH3 domain with the GK domain (20,22). Collectively these findings indicate the physiological importance of the SH3-GK domain interaction, but a molecular function of this interaction remains to be established.Tyrosine phosphorylation of NR2B (26, 27) is augmented on LTP induction (28, 29), and several observations suggest that up-regulation of NMDA receptor activity by Src-mediated tyrosine phosphorylation is an important step in the induction of LTP. 1) Src increases NMDA receptor activity (30 -32) by elevating its peak current (33), 2) the activity of Src is up-regulated during LTP (34), 3) inhibition of Src can prevent LTP (30), and 4) an increase in synaptic transmission on Src activation occludes subsequent LTP induction (34).It is well established that Src can be activated by another tyrosine kinase, Pyk2/CAK␤/CADTK (35-38). Pyk2 is stimulated upon Ca 2ϩ influx, activation of PKC by phorbol esters, or stimulation of G q -linked receptors such as the muscarinic acetylcholine receptor M1 or the metabotropic glutamate receptor mGluR1 (35, 37, 39 -48). Neither Ca 2ϩ nor PKC appear to directly regulate Pyk2 in vitro (39); how Ca 2ϩ or PKC activates Pyk2 in vivo is unknown. When stimulated, Pyk2 autophosphorylates itself on tyrosine 402. The...

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Characterization of glutamate receptor interacting protein-immunopositive neurons in cerebellum and cerebral cortex of the albino rat

Cited by 38 publications

References 61 publications

Voltage-Controlled Plasticity at GluR2-Deficient Synapses Onto Hippocampal Interneurons

Voltage-Controlled Plasticity at GluR2-Deficient Synapses Onto Hippocampal Interneurons

Group I Metabotropic Glutamate Receptor NMDA Receptor Coupling and Signaling Cascade Mediate Spinal Dorsal Horn NMDA Receptor 2B Tyrosine Phosphorylation Associated with Inflammatory Hyperalgesia

Interaction of the Tyrosine Kinase Pyk2 with the N-Methyl-d-aspartate Receptor Complex via the Src Homology 3 Domains of PSD-95 and SAP102

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