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PLoS One. 2017 Feb 2;12(2):e0171489. doi: 10.1371/journal.pone.0171489. eCollection 2017.

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

Author information

1
Department of Biosciences, Division of Biochemistry and Biotechnology, University of Helsinki, Helsinki, Finland.
2
Turku Centre for Biotechnology, Åbo Akademi University and University of Turku, Turku, Finland.
3
A.I. Virtanen Institute, University of Eastern Finland, Kuopio, Finland.

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.

PMID:
28152104
PMCID:
PMC5289633
DOI:
10.1371/journal.pone.0171489
[Indexed for MEDLINE]
Free PMC Article

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