Negative regulation of NMDA receptor-mediated neuronal transmission

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Homo sapiens
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The duration of NMDA receptor-mediated neuronal transmission can be limited by binding of the activated calmodulin to the activated NMDA receptor. In addition to shortening the NMDA channel pore open state, calmodulin interferes with ACTN2-mediated anchoring of NMDA receptors to the postsynaptic density (Ehlers et al. 1996, Wyszynski et al. 1997). Protein phosphatases PPM1E and PPM1F dephosphorylate activated calcium/calmodulin-dependent kinases (CaMKs), thus halting CaMK-mediated signaling (Ishida, Okuno et al. 1998, Ishida et al. 1998, Kitani et al. 2003).

Literature References
PubMed ID Title Journal Year
9442023 A novel protein phosphatase that dephosphorylates and regulates Ca2+/calmodulin-dependent protein kinase II

Ishida, A, Fujisawa, H, Kameshita, I

J. Biol. Chem. 1998
9009191 Competitive binding of alpha-actinin and calmodulin to the NMDA receptor

Beggs, AH, Wyszynski, M, Lin, J, Craig, AM, Sheng, M, Nigh, E, Rao, A

Nature 1997
8625412 Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit

Bernhadt, JP, Zhang, S, Huganir, RL, Ehlers, MD

Cell 1996
9875237 Regulation of multifunctional Ca2+/calmodulin-dependent protein kinases by Ca2+/calmodulin-dependent protein kinase phosphatase

Ishida, A, Fujisawa, H, Kitani, T, Kameshita, I, Okuno, S

Biochem. Biophys. Res. Commun. 1998
12807427 Subcellular distributions of rat CaM kinase phosphatase N and other members of the CaM kinase regulatory system

Fujisawa, H, Okuno, S, Kitani, T, Takeuchi, M

J. Neurochem. 2003
Cross References
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