1996
DOI: 10.1016/s0092-8674(00)81053-3
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Interaction of Nitric Oxide Synthase with the Postsynaptic Density Protein PSD-95 and α1-Syntrophin Mediated by PDZ Domains

Abstract: Neuronal nitric oxide synthase (nNOS) is concentrated at synaptic junctions in brain and motor endplates in skeletal muscle. Here, we show that the N-terminus of nNOS, which contains a PDZ protein motif, interacts with similar motifs in postsynaptic density-95 protein (PSD-95) and a related novel protein, PSD-93.nNOS and PSD-95 are coexpressed in numerous neuronal populations, and a PSD-95/nNOS complex occurs in cerebellum. PDZ domain interactions also mediate binding of nNOS to skeletal muscle syntrophin, a d… Show more

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Cited by 1,523 publications
(1,232 citation statements)
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References 37 publications
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“…The sequences of these clones showed that they code for truncated forms of already known proteins. The product of clone 15 is highly homologous to the PSD-95 protein (Brenman et al, 1996) and that of clone 43 to the b1-syntrophin (Ahn et al, 1994). Clone 15 encodes a protein including only the PDZ1 and PDZ2 domains, but lacking the PDZ3, SH3 and guanylate kinase domains present in the carboxy-terminal part of PSD-95.…”
Section: Binding Of Tax To Pdz Proteinsmentioning
confidence: 99%
See 1 more Smart Citation
“…The sequences of these clones showed that they code for truncated forms of already known proteins. The product of clone 15 is highly homologous to the PSD-95 protein (Brenman et al, 1996) and that of clone 43 to the b1-syntrophin (Ahn et al, 1994). Clone 15 encodes a protein including only the PDZ1 and PDZ2 domains, but lacking the PDZ3, SH3 and guanylate kinase domains present in the carboxy-terminal part of PSD-95.…”
Section: Binding Of Tax To Pdz Proteinsmentioning
confidence: 99%
“…It has been veri®ed for all the clones of this study that the interaction with Tax was mediated by the PDZ domain. The observation that nNOS and PSD-95 interact through their PDZ domains has shown that these motifs also exhibit protein surface interactions (Brenman et al, 1996). The internal domain of Tax involved in the interaction for clones 2, 40 and 43 could present a particular surface motif permitting association with the PDZ domain.…”
Section: Interaction Of the Viral Protein Tax With Pdz Proteinsmentioning
confidence: 99%
“…Skeletal muscles express two alternatively spliced nNOS isoforms, nNOSμ and nNOSβ, both of which are expressed in fast and slow muscle types (Silvagno et al 1996;Stamler and Meissner 2001;Percival et al 2010, Figure 1). nNOSμ is scaffolded to the subsarcolemmal dystrophin glycoprotein complex (DGC) and neuromuscular junction (Brenman et al 1995(Brenman et al , 1996Adams et al 2000). The sarcolemmal nNOSμ association requires α-syntrophin, dystrophin, and α-dystrobrevin (Brenman et al 1995(Brenman et al , 1996Grady et al 2000;Adams et al 2000Adams et al , 2008.…”
Section: Introductionmentioning
confidence: 99%
“…nNOSμ is scaffolded to the subsarcolemmal dystrophin glycoprotein complex (DGC) and neuromuscular junction (Brenman et al 1995(Brenman et al , 1996Adams et al 2000). The sarcolemmal nNOSμ association requires α-syntrophin, dystrophin, and α-dystrobrevin (Brenman et al 1995(Brenman et al , 1996Grady et al 2000;Adams et al 2000Adams et al , 2008. In mice, nNOSμ is not only localized at the sarcolemma, but is also normally expressed at relatively high levels in the cytoplasm (Chang et al 1996;Kameya et al 1999;Thomas et al 2003).…”
Section: Introductionmentioning
confidence: 99%
“…They described how the N-methyl-D-aspartate (NMDA) receptor is S-nitrosated by neuronal NOS [30] via postsynaptic density protein 95 (PSD95), which serves as a scaffold. PSD95 is known to interaction with both the neuronal NOS [31] as well as the NMDA receptor [32], supporting its role as a scaffold. However, whether disrupting PSD95 interactions alters S-nitrosation of NMDA receptor remains unclear.…”
Section: Enzymatic Regulation Of Protein S-nitrosationmentioning
confidence: 95%