Cysteine 893 is a target of regulatory thiol modifications of GluA1 AMPA receptors

von Ossowski, L., Li, L-L., Moykkynen, T., Coleman, S.K., Courtney, M.J. and Keinänen, K. (2017) Cysteine 893 is a target of regulatory thiol modifications of GluA1 AMPA receptors. PLoS One, 12 (2). e0171489. ISSN 1932-6203

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Recent studies indicate that glutamatergic signaling involves, and is regulated by, thiol modifying and redox-active compounds. In this study, we examined the role of a reactive cysteine residue, Cys-893, in the cytosolic C-terminal tail of GluA1 AMPA receptor as a potential regulatory target. Elimination of the thiol function by substitution of serine for Cys-893 led to increased steady-state expression level and strongly reduced interaction with SAP97, a major cytosolic interaction partner of GluA1 C-terminus. Moreover, we found that of the three cysteine residues in GluA1 C-terminal tail, Cys-893 is the predominant target for S-nitrosylation induced by exogenous nitric oxide donors in cultured cells and lysates. Co-precipitation experiments provided evidence for native association of SAP97 with neuronal nitric oxide synthase (nNOS) and for the potential coupling of Ca2+-permeable GluA1 receptors with nNOS via SAP97. Our results show that Cys-893 can serve as a molecular target for regulatory thiol modifications of GluA1 receptors, including the effects of nitric oxide.

Item Type: Article
Additional Information: The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Uncontrolled Keywords: AMPA receptor, cysteine, S-nitrosylation, PSD-95, SAP97;
Subjects: University of Westminster > Science and Technology
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Date Deposited: 07 Feb 2017 15:45
Last Modified: 07 Feb 2017 15:45

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