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They were starved in media without FBS for 4 hours and stimulated with 10 nM hormones for 15 min. We prepared six separate wells for each treatment, i.e. control non-stimulated cells and cells stimulated with insulin, IGF-1 and with 1Ins. The samples were evenly distributed on four six-well plates. The cells were lysed in freshly prepared, preheated (95 °C) 4% deoxycholate, 100 mM Tris/Cl buffer pH 8.5. The samples were ultrasonicated using a probe (Bandelin Sonoplus) for 10 s at 70% intensity and heated at 95 °C for 5 min twice. The protein lysates were reduced using 10 mM tris(2-carboxyethyl)phosphine (TCEP) and alkylated with 40 mM chloroacetamide and digested overnight with LysC/trypsin in 1:50 enzyme:protein ratio. Phosphopeptide enrichment of 350 ug protein per condition was performed using TiO2 beads (Titansphere Phos-TiO bulk, 10 μm) following established protocol without automation (1). Phosphopeptides were separated and analyzed by LC-MS/MS. LC separation was performed on Dionex Ultimate 3000 nano HPLC system online connected with MS instrument. Samples were loaded onto the trap column (C18 PepMap100, 5 μm particle size, 300 μm x 5 mm, Thermo Scientific) for 2 min at 25 μl/min. Loading buffer was composed of water, 2% acetonitrile and 0.1% trifluoroacetic acid. Peptides were eluted with Mobile phase B gradient from 5% to 30% B for 72 min. Mobile phase buffer A was composed of water and 0.1% formic acid. Mobile phase B was composed of acetonitrile and 0.1% formic acid. Nano reversed phase column (Aurora Ultimate TS, 25 cm x 75 μm ID, 1.7 μm particle size, Ion Opticks) was used for LC/MS analysis.  Peptide mixture was analyzed on Thermo Scientific Orbitrap Fusion Lumos by data independent approach. Eluting peptide cations were converted to gas-phase ions by electrospray ionization in Positive mode. Spray voltage was set to 1600 V and ion transfer tube temperature to 275 °C. MS1 scans of peptide precursors were analyzed in Orbitrap in range 350-1300 m/z at 60K resolution and with following settings: RF Lens 30%, maximum injection time 118 ms, AGC target 100. DIA scans were performed in Orbitrap at 30K resolution. AGC target was set to 1000 and maximum injection time mode to Auto. Precursor mass range 400-1000 m/z was covered by 30 windows 20 Da wide. Activation type was set to HCD with 33% collision energy. (1) Humphrey SJ, Karayel O, James DE, Mann M. High-throughput and high-sensitivity phosphoproteomics with the EasyPhos platform. Nature Protocols. 2018;13(9):1897–916."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The acquired dataset was analyzed using Spectronaut version 19.8.250311.62635 (2). The analysis workflow employed was directDIA+(Deep) with normalisation, incorporating Post-Translational Modifications (PTM) Analysis with the multiplicity option enabled. The analysis was performed using a human proteome database (one protein per gene), which was downloaded in November 2024 and included common contaminants. Search parameters were as follows: trypsin enzyme specificity, with Carbamidomethyl (C) as a fixed modification, and Acetyl (protein N-term), Oxidation (M), and Phosphorylation (STY) as variable modifications. The thresholds for Peptide Spectrum Match (PSM) and protein False Discovery Rate (FDR) were set to 0.01, while the minimum PTM Localization Threshold was set to 0.75.  The resulting data were further processed using Perseus 1.6.15 (3). Phosphorylation sites quantifies in all 6 replicates in at least one goup were considered valid. Missing values were replaced from normal distribution (width 0.3, down shift 1.8). To identify differentially expressed phosphorylation sites two-sample t-test was performed with s0=0.75. To account for multiple-hypothesis testing, a permutation-based FDR of 0.15 was applied to the dataset. Kinase-substrate relations and regulatory sites and were extracted from PhosphoSitePlus (4).  (2) Bruderer R, Bernhardt OM, Gandhi T, Miladinović SM, Cheng L-Y, Messner S, et al. Extending the Limits of Quantitative Proteome Profiling with Data-Independent Acquisition and Application to Acetaminophen-Treated Three-Dimensional Liver Microtissues*[S]. Molecular & Cellular Proteomics. 2015;14(5):1400–10. (3) Tyanova S, Temu T, Sinitcyn P, Carlson A, Hein MY, Geiger T, et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat Methods. 2016;13(9):731–40. (4) Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, Murray B, et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 2012;40(Database issue):D261–70."],"omics_type":["Proteomics"],"labhead":["Jiri Jiracek"],"instrument_platform":[""],"labhead_affiliation":["Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 16610 Praha 6, Czech Republic"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["jana.brezinova@uochb.cas.cz"],"publication":["Not available"],"submitter_affiliation":["Institute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n. 2,\nPrague, 166 10, Czech Republic"],"submitter_country":["Czech Republic"],"additional_accession":[]},"is_claimable":false,"name":"An engineered insulin analog with dual insulin and IGF-1 receptor agonism and distinct signaling","description":"Insulin and insulin-like growth factors (IGF-1 and IGF-2) regulate metabolism, growth, and development via related receptors. In contexts such as brain function or fetal development, coordinated signaling by all three hormones is essential. We report the engineering of [GluB10, D-HisB24, GlyB31, TyrB32]-insulin (1Ins), an analog with high affinity for IR-A, IR-B, and especially IGF-1R. 1Ins binds IGF-1R ~1,000-fold more strongly than native insulin, approaching IGF-1 levels. CryoEM structures reveal how minimal substitutions in 1Ins enable effective binding to both IR-A and IGF-1R. In neuronal cells, 1Ins robustly activates both IR and IGF-1R pathways, promotes survival, and exceeds native ligands in neuroprotective assays. In vivo, 1Ins regulates glucose effectively in mice and rats. Phosphoproteomic profiling confirms dual pathway activation and identifies targets unique to 1Ins. These findings demonstrate that rational design of dual-receptor agonists can yield potent, versatile ligands with therapeutic promise in metabolic control, neuroprotection, and 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