TY - JOUR
T1 - CAPON
T2 - A protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95
AU - Jaffrey, Samie R.
AU - Snowman, Adele M.
AU - Eliasson, Mikael J.L.
AU - Cohen, Noam A.
AU - Snyder, Solomon H.
N1 - Funding Information:
We thank M. Kennedy for kindly providing a PSD95 cDNA; E. Fung, C. Lowenstein, T. Michel, J. Brenman, and D. Bredt for plasmids; E. Fung for yeast strains; and A. Lanahan and P. Worley for the rat hippocampal cDNA library. M. J. L. E. is a recipient of a Gustavus and Louise Pfeiffer Scholarship. S. R. J. is supported by training grant GM-07309. N. A. C. is supported by training grant MH-10341. This work was supported by USPHS grant DA00074 and a Research Scientist Award, MH-18501, to S. H. S.
PY - 1998/1
Y1 - 1998/1
N2 - Nitric oxide (NO) produced by neuronal nitric oxide synthase (nNOS) is important for N-methyl-D-aspartate (NMDA) receptor-dependent neurotransmitter release, neurotoxicity, and cyclic GMP elevations. The coupling of NMDA receptor-mediated calcium influx and nNOS activation is postulated to be due to a physical coupling of the receptor and the enzyme by an intermediary adaptor protein, PSD95, through a unique PDZ-PDZ domain interaction between PSD95 and nNOS. Here, we report the identification of a novel nNOS-associated protein, CAPON, which is highly enriched in brain end has numerous colocalizations with nNOS. CAPON interacts with the nNOS PDZ domain through its C terminus. CAPON competes with PSD95 for interaction with nNOS, and overexpression of CAPON results in a loss of PSD95/nNOS complexes in transfected cells. CAPON may influence nNOS by regulating its ability to associate with PSD95/NMDA receptor complexes.
AB - Nitric oxide (NO) produced by neuronal nitric oxide synthase (nNOS) is important for N-methyl-D-aspartate (NMDA) receptor-dependent neurotransmitter release, neurotoxicity, and cyclic GMP elevations. The coupling of NMDA receptor-mediated calcium influx and nNOS activation is postulated to be due to a physical coupling of the receptor and the enzyme by an intermediary adaptor protein, PSD95, through a unique PDZ-PDZ domain interaction between PSD95 and nNOS. Here, we report the identification of a novel nNOS-associated protein, CAPON, which is highly enriched in brain end has numerous colocalizations with nNOS. CAPON interacts with the nNOS PDZ domain through its C terminus. CAPON competes with PSD95 for interaction with nNOS, and overexpression of CAPON results in a loss of PSD95/nNOS complexes in transfected cells. CAPON may influence nNOS by regulating its ability to associate with PSD95/NMDA receptor complexes.
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U2 - 10.1016/S0896-6273(00)80439-0
DO - 10.1016/S0896-6273(00)80439-0
M3 - Article
C2 - 9459447
AN - SCOPUS:0031932281
SN - 0896-6273
VL - 20
SP - 115
EP - 124
JO - Neuron
JF - Neuron
IS - 1
ER -