| Title | Cysteine 893 is a target of regulatory thiol modifications of GluA1 AMPA receptors |
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| Type | Journal article |
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| Authors | von Ossowski, L., Li, L-L., Moykkynen, T., Coleman, S.K., Courtney, M.J. and Keinänen, K. |
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| Abstract | 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. |
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| Keywords | AMPA receptor, cysteine, S-nitrosylation, PSD-95, SAP97 |
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| Article number | e0171489 |
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| Journal | PLoS ONE |
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| Journal citation | 12 (2) |
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| ISSN | 1932-6203 |
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| Year | 2017 |
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| Publisher | Public Library of Science |
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| Publisher's version | |
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| Digital Object Identifier (DOI) | https://doi.org/10.1371/journal.pone.0171489 |
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| PubMed ID | 28152104 |
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| Publication dates |
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| Published | 02 Feb 2017 |
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| Funder | Magnus Ehrnrooth Foundation |
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| Alfred Kordelin Foundation |
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| Orion Research Foundation |
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| License | CC BY 4.0 |
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