{"database":"GEO","file_versions":[],"scores":null,"additional":{"omics_type":["Transcriptomics"],"species":["Homo sapiens"],"gds_type":["Expression profiling by high throughput sequencing"],"full_dataset_link":["https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE286543"],"repository":["GEO"],"entry_type":["GSE"],"additional_accession":[]},"is_claimable":false,"name":"Nitric oxide drives proteomic diversity through alternative splicing [CLIP-Seq]","description":"Redox signaling by nitric oxide (NO) is estimated to control the large part of the global proteome via S-nitrosylation (SNO-modification). Here we report that RNA-binding proteins (RBPs) represent the most significantly enriched class of S-nitrosylation targets, with broad coverage of spliceosomal factors. We demonstrate that NO regulates alternative splicing (AS) and that S-nitrosylation of PTBP1, a central regulator of AS, can massively shift and contextually alter gene expression, while further enriching the transcriptome for SNO sites. PTBP1 S-nitrosylation changes RNA-binding domain conformation, RNA motif recognition, protein–RNA and protein–protein interactions, and intracellular trafficking to impact pathways for viral infection and neurodegeneration. Levels of SNO-PTBP1 are reduced in mouse and human Alzheimer’s brains and correlate with adverse clinical outcomes. Overall, SNO-RBPs are characterized by conservation across diverse lineages and SNO sites and provide a blueprint for redox regulation of both transcriptome and proteome in physiology and disease.","dates":{"publication":"2026/05/21"},"accession":"GSE286543","cross_references":{"GSM":["GSM8729057","GSM8729068","GSM8729056","GSM8729067","GSM8729066","GSM8729055","GSM8729065","GSM8729059","GSM8729069","GSM8729058","GSM8729060","GSM8729070","GSM8729064","GSM8729063","GSM8729062","GSM8729061"],"GPL":["21697"],"GSE":["286543"],"taxon":["Homo sapiens"],"PMID":["[42167237]"]}}