S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis

Balakrishnan Selvakumar; Meagan A. Jenkins; Natasha K. Hussain; Richard L. Huganir; Stephen F. Traynelis; Solomon H. Snyder

doi:10.1073/pnas.1221295110

S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis

Balakrishnan Selvakumar, Meagan A. Jenkins, Natasha K. Hussain, Richard L. Huganir, Stephen F. Traynelis, Solomon H. Snyder

Research output: Contribution to journal › Article › peer-review

Abstract

NMDA receptor activation can elicit synaptic plasticity by augmenting conductance of the AMPA receptor GluA1 subsequent to phosphorylation at S831 by Ca²⁺-dependent kinases. NMDA receptor activation also regulates synaptic plasticity by causing endocytosis of AMPA receptor GluA1. We demonstrate a unique signaling cascade for these processes mediated by NMDA receptor-dependent NO formation and GluA1 S-nitrosylation. Thus, S-nitrosylation of GluA1 at C875 enhances S831 phosphorylation, facilitates the associated AMPA receptor conductance increase, and results in endocytosis by increasing receptor binding to the AP2 protein of the endocytotic machinery.

Original language	English (US)
Pages (from-to)	1077-1082
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	110
Issue number	3
DOIs	https://doi.org/10.1073/pnas.1221295110
State	Published - Jan 15 2013
Externally published	Yes

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S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis. / Selvakumar, Balakrishnan; Jenkins, Meagan A.; Hussain, Natasha K.; Huganir, Richard L.; Traynelis, Stephen F.; Snyder, Solomon H.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, No. 3, 15.01.2013, p. 1077-1082.

Research output: Contribution to journal › Article › peer-review

Selvakumar, Balakrishnan ; Jenkins, Meagan A. ; Hussain, Natasha K. ; Huganir, Richard L. ; Traynelis, Stephen F. ; Snyder, Solomon H. / S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis. In: Proceedings of the National Academy of Sciences of the United States of America. 2013 ; Vol. 110, No. 3. pp. 1077-1082.

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abstract = "NMDA receptor activation can elicit synaptic plasticity by augmenting conductance of the AMPA receptor GluA1 subsequent to phosphorylation at S831 by Ca2+-dependent kinases. NMDA receptor activation also regulates synaptic plasticity by causing endocytosis of AMPA receptor GluA1. We demonstrate a unique signaling cascade for these processes mediated by NMDA receptor-dependent NO formation and GluA1 S-nitrosylation. Thus, S-nitrosylation of GluA1 at C875 enhances S831 phosphorylation, facilitates the associated AMPA receptor conductance increase, and results in endocytosis by increasing receptor binding to the AP2 protein of the endocytotic machinery.",

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AU - Traynelis, Stephen F.

AU - Snyder, Solomon H.

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AB - NMDA receptor activation can elicit synaptic plasticity by augmenting conductance of the AMPA receptor GluA1 subsequent to phosphorylation at S831 by Ca2+-dependent kinases. NMDA receptor activation also regulates synaptic plasticity by causing endocytosis of AMPA receptor GluA1. We demonstrate a unique signaling cascade for these processes mediated by NMDA receptor-dependent NO formation and GluA1 S-nitrosylation. Thus, S-nitrosylation of GluA1 at C875 enhances S831 phosphorylation, facilitates the associated AMPA receptor conductance increase, and results in endocytosis by increasing receptor binding to the AP2 protein of the endocytotic machinery.

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S-nitrosylation of AMPA receptor GluA1 regulates phosphorylation, single-channel conductance, and endocytosis

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