biostudies-literatureUnknown14(1)Palollathil A<h4>Background</h4>Fibroblast growth factor receptors (FGFRs) play a crucial role in tissue homeostasis and organ development by regulating cellular processes, including proliferation, differentiation, and survival. Dysregulation of FGFRs contributes to developmental disorders and carcinogenesis. As membrane-bound receptors, they represent promising targets for therapeutic intervention and drug development.<h4>Methods</h4>This study employed a systematic in silico analysis of publicly available phosphoproteomics datasets to provide a comprehensive overview of the phosphorylation regulatory network of the FGFR family.<h4>Results</h4>We identified predominant phosphosites in FGFR1-4 that exhibited differential abundance across diverse experimental conditions, specifically, Y653 in FGFR1; S45Proteomes8https://www.ebi.ac.uk/biostudies/studies/S-EPMC12922108biostudies-literatureProteome-Wide Analysis of Functional Phosphosites in the FGFR Family of Proteins: Insights from Large-Scale Phosphoproteomic Analysis.PMC12922108Sambreena ABasthikoppa Shivamurthy PPoojari TRPerunelly Gopalakrishnan APalollathil AMahin ARaju RfalseProteome-Wide Analysis of Functional Phosphosites in the FGFR Family of Proteins: Insights from Large-Scale Phosphoproteomic Analysis.<h4>Background</h4>Fibroblast growth factor receptors (FGFRs) play a crucial role in tissue homeostasis and organ development by regulating cellular processes, including proliferation, differentiation, and survival. Dysregulation of FGFRs contributes to developmental disorders and carcinogenesis. As membrane-bound receptors, they represent promising targets for therapeutic intervention and drug development.<h4>Methods</h4>This study employed a systematic in silico analysis of publicly available phosphoproteomics datasets to provide a comprehensive overview of the phosphorylation regulatory network of the FGFR family.<h4>Results</h4>We identified predominant phosphosites in FGFR1-4 that exhibited differential abundance across diverse experimental conditions, specifically, Y653 in FGFR1; S452026-01-01T00:00:00Z2026 Feb2026-07-09T11:43:20.617Z2026-07-09T10:55:39.767ZS-EPMC129221084171809010.3390/proteomes14010008