Domain Interaction Between NMDA Receptor Subunits and the Postsynaptic Density Protein PSD-95

Kornau, Hans Christian; Schenker, Leslie T.; Kennedy, Mary B.; Seeburg, Peter H.

doi:10.1126/science.7569905

Cited by 1,789 publications

(1,462 citation statements)

References 39 publications

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“…The PDZ domain is now known to be present in a rapidly expanding group of proteins (Ponting and Phillips, 1995) and is also called Discs-large Homology Region (DHR) or GLGF repeat. It is shown here that Tax interacts with cellular proteins via their PDZ domains and that this binding involves the C-terminus of Tax which ®ts with the S/TXV-COOH consensus sequence previously de®ned for cellular trans-membrane receptors interacting with PDZ proteins such as PSD-95 (Kornau et al, 1995). Mutagenesis analysis of this Tax motif demonstrated its importance for the binding of several of the PDZ proteins identi®ed in this study.…”

Section: Introductionsupporting

confidence: 60%

“…The ®rst two PDZ domains of PSD-95 have been shown to interact with the cytoplasmic tails of subunits of the NMDA glutamate receptor and of Shaker-type K + channels (Kim et al, 1995;Kornau et al, 1995;Niethammer et al, 1996). It has also been shown that the PDZ domains of FAP-1 mediate interaction with the C-terminus of Fas (Sato et al, 1995).…”

Section: Mapping Of the Domains Of Tax Mediating Interaction With Thementioning

confidence: 99%

“…It has also been shown that the PDZ domains of FAP-1 mediate interaction with the C-terminus of Fas (Sato et al, 1995). Determination of the sequence requirement in NMDA receptor NR2 subunits has led to the proposal of the following consensus sequence: T/SXV-COOH (Kornau et al, 1995). A detailed analysis by site-directed mutagenesis of the sequence of the C-terminus of the shaker-type Kv 1.4 channel required for the interaction with PSD-95 has clearly shown the importance of the carboxyterminal valine (Kim et al, 1995), thereafter referred as position 0, and of the threonine at position 72.…”

Section: Mapping Of the Domains Of Tax Mediating Interaction With Thementioning

confidence: 99%

“…However, it could exert other currently unknown functions through its PDZ domain. PSD-95 has been shown to interact with the intracellular tail of subunits of the glutamate receptor and of shaker-type K + channels (Kim et al, 1995;Kornau et al, 1995). This interaction is likely to play an important role in the clustering of receptors at the membrane (Gomperts, 1996).…”

Section: Identi®cation Of New Human Cellular Proteins With Pdz Domainsmentioning

confidence: 99%

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The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

et al. 1998

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Infection by HTLV-1 has been correlated with the appearance of various proliferative or degenerative diseases. Some of these disorders have been observed in transgenic mice expressing the Tax protein, which is known to transactivate various viral and cellular promoters through interactions with several transcription factors. In this study we show that the C-terminus of this viral oncoprotein represents a motif permitting binding of Tax to the PDZ domains of several cellular proteins. A two-hybrid screen with Tax as bait indeed yielded complementary DNAs coding for six proteins including PDZ domains. Two of them correspond to truncated forms of the PSD-95 and b1-syntrophin proteins, another clone codes for a protein homologous to the product of the C. elegans gene lin-7. The other three clones code for new human members of the PDZ family of cellular proteins. The interaction of Tax with the products of these clones was con®rmed by immunoprecipitation assays in mammalian cells, and analysis of various mutants of Tax established the importance of the Cterminal amino acids for several of these interactions. These data suggest that Tax could perturb the normal function of targeted cellular proteins by strongly interacting with their PDZ domains.

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Section: Introductionsupporting

confidence: 60%

Section: Mapping Of the Domains Of Tax Mediating Interaction With Thementioning

confidence: 99%

Section: Mapping Of the Domains Of Tax Mediating Interaction With Thementioning

confidence: 99%

Section: Identi®cation Of New Human Cellular Proteins With Pdz Domainsmentioning

confidence: 99%

See 2 more Smart Citations

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

et al. 1998

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“…The PDZ domain is a module of about 90 amino acids designed to bind to other proteins (Sheng and Sala, 2001). One of the first PDZ proteins discovered, PSD-95, was shown to bind directly to the C-terminus of NR2 subunits in NMDA receptors and induced clustering of the receptors in cotransfected cells (Kornau et al, 1995;Niethammer et al, 1996). Whether PSD-95 is responsible for positioning native NMDA receptors at synapses in vivo is an open question, but it is clear that the protein can function as an organizing scaffold that tethers other components to the receptors (Tomita et al, 2001;Hung and Sheng, 2002).…”

Section: Localization Of Nicotinic Receptors On Neuronsmentioning

confidence: 99%

Nicotinic α7 receptors: Synaptic options and downstream signaling in neurons

2002

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Nicotinic receptors are cation-ion selective ligand-gated ion channels that are expressed throughout the nervous system. Most have significant calcium permeabilities, enabling them to regulate calcium-dependent events. One of the most abundant is a species composed of the ␣7 gene product and having a relative calcium permeability equivalent to that of NMDA receptors. The ␣7-containing receptors can be found presynaptically where they modulate transmitter release, and postsynaptically where they generate excitatory responses. They can also be found in perisynaptic locations where they modulate other inputs to the neuron and can activate a variety of downstream signaling pathways. The effects the receptors produce depend critically on the sites at which they are clustered. Instructive preparations for examining ␣7-containing receptors are the rat hippocampus, where they are thought to play a modulatory role, and the chick ciliary ganglion, where they participate in throughput transmission as well as regulatory signaling. Relatively high levels of ␣7-containing receptors are found in the two preparations, and the receptors display a variety of synaptic options and functions in the two cases. Progress is starting to be made in understanding the mechanisms responsible for localizing the receptors at specific sites and in identifying components tethered in the vicinity of the receptors that may facilitate signal transduction and downstream signaling.

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Immunocytochemical localization of the GABAC receptor ? subunits in the cat, goldfish, and chicken retina

et al. 1997

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Polyclonal antibodies against the N-terminus of the rat rho1 subunit were used to study the distribution of gamma-aminobutyric acid C (GABA(C)) receptors in the cat, goldfish, and chicken retina. Strong punctate immunoreactivity was present in the inner plexiform layer (IPL) of all three species. The punctate labelling suggests a clustering of the GABA(C) receptors at synaptic sites. Weak label was also found in the outer plexiform layer (OPL) and over the cell bodies of bipolar cells. Double immunostaining of vertical sections with an antibody against protein kinase C (PKC) showed the punctate immunofluorescence to colocalize with bipolar cell axon terminals. In the goldfish retina, the axon terminals of Mb1 bipolar cells were enclosed by rho-immunoreactive puncta. In the chicken retina, several distinct strata within the IPL showed a high density of rho-immunoreactive puncta. The results suggest a high degree of sequence homology between the rho subunits of different vertebrate species, and they show that the retinal localization of GABA(C) receptors is similar across different species.

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Domain Interaction Between NMDA Receptor Subunits and the Postsynaptic Density Protein PSD-95

Cited by 1,789 publications

References 39 publications

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

Nicotinic α7 receptors: Synaptic options and downstream signaling in neurons

Immunocytochemical localization of the GABAC receptor ? subunits in the cat, goldfish, and chicken retina

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