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Proteomic analysis of S-nitrosylated nuclear proteins in rat cortical neurons

Smith, JG; Aldous, SG; Andreassi, C; Cuda, G; Gaspari, M; Riccio, A; (2018) Proteomic analysis of S-nitrosylated nuclear proteins in rat cortical neurons. Science Signaling , 11 (537) , Article eaar3396. 10.1126/scisignal.aar3396. Green open access

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Abstract

The ability of neurons to modulate gene expression in response to extrinsic signals is necessary for proper brain function. S-nitrosylation is the covalent attachment of a nitric oxide (NO) moiety to cysteine thiols and is critical for transducing extracellular stimuli into specific patterns of gene expression. In the cerebral cortex, S-nitrosylation of histone deacetylase 2 (HDAC2) is required for gene transcription during neuronal development, however only few nuclear targets of Snitrosylation have been identified to date. Here, we used S-nitrosothiol Resin Assisted Capture (SNORAC) coupled with mass spectrometry analysis to identify 614 S-nitrosylated nuclear proteins. Of these, 131 proteins had never been shown to be S-nitrosylated in any system, and 612 are new targets of S-nitrosylation in neurons. The site(s) of S-nitrosylation were identified for 59% of the targets, and motifs containing single lysines found at 33% of these sites. In addition, lysine motifs were found to be necessary for promoting S-nitrosylation of HDAC2 and Methyl-CpG Binding Protein 3 (MBD3). Moreover, S-nitrosylation of the histone binding protein RBBP7 was found to be necessary for dendritogenesis. Overall, our study provides the first extensive characterization of Snitrosylated nuclear proteins in neurons and identifies putative S-nitrosylation motifs that may be shared with other targets of nitric oxide signaling.

Type: Article
Title: Proteomic analysis of S-nitrosylated nuclear proteins in rat cortical neurons
Open access status: An open access version is available from UCL Discovery
DOI: 10.1126/scisignal.aar3396
Publisher version: https://doi.org/10.1126/scisignal.aar3396
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Cell Biology, biotin-switch technique, cell-death, stress, recognition, complex, identification, translocation, transcription, expression, migration
UCL classification: UCL
UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology > Neurodegenerative Diseases
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL
URI: https://discovery.ucl.ac.uk/id/eprint/10057220
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