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These were processed by single-pot, solid phase proteomics sample preparation (SP3) on an Agilent Bravo LT96 liquid handling platform(97) using Sera-mag beads (Cytiva cat # 44152105050250 and 24152105050250 mixed 1:1). 7 µg of proteins were processed with a 10:1 w/w ratio of beads to proteins and 18 minutes binding time. Reduction was performed with 2.5 mM dithiothreitol for 30 minutes at 37 °C, followed by alkylation with 5 mM iodoacedamide for 30 minutes at 37 °C. The proteins were then digested with trypsin overnight at 37 °C. Peptides were injected for each liquid chromatography-mass spectrometry (LC-MS) acquisition. The LC-MS platform consisted of a Vanquish Neo system (Thermo Fisher Scientific) connected to an Orbitrap Astral mass spectrometer (Thermo Fisher Scientific) operating under Tune 2.0.690.17. Mobile phases consisted of 0.1% v/v formic acid in water (mobile phase A) and 0.1% formic acid in 80% acetonitrile/water v/v (mobile phase B). The system was set up in trap-and-elute workflow with a pepmap Neo trap cartridge (Thermo Fisher Scientific cat # 174500). The samples were acquired with a 40-sample per day method and separated on an EASY-Spray PepMap Neo column (150 µm x 15 cm) (Thermo Fisher Scientific cat # ES906) with a 33 minute gradient employing a linear separation between 8%-22.5% B at 800 nl/min in 24 minutes.  MS acquisitions were performed in narrow-window data-independent (DIA) mode(98). MS1 spectra were acquired with a resolution of 240000 and 5 ms maximum injection time with a full scan range of 380–980 m/z and automatic gain control of 500%. Source RF lens was set to 40%. The DIA part was performed with 300 windows of 2-Th scanning from 380 to 980 m/z under a time control of 0.6 second maximum second per duty cycle. The ion injection time was set to a maximum of 3ms per windows and the automatic gain control target to 500% (50000 ions). The isolated ions were fragmented using HCD with 25% Normalized Collision Energy."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The resulting raw files were processed with DIA-NN 2.3.0(99) using an in silico spectral library generated by DIA-NN from R. norvegicus UniProt (including TrEMBL, all isoforms and common MS contaminants). The spectral library is included in the data deposition. The spectral library included methionine oxidation, 1 missed cleavage, precursor charge states 1-4 and common contaminants. The data was searched with a minimum peptide length of 7, 1 missed cleavage, methionine oxidation as variable modification, cysteine carbamidomethylation as fixed modification, match between runs, and the direct quantification option in DIA-NN. Normalization was disabled. Proteotypicity was set to genes. The data was filtered with a 0.01 q-value filter at the precursor level and 1% false discovery rate (FDR) at the protein group level."],"omics_type":["Proteomics"],"labhead":["Andrea Graziadei"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Human Technopole"],"species":["Rattus Norvegicus (rat)"],"publication":["10.64898/2026.07.04.736497"],"submitter_mail":["andrea.graziadei@fht.org"],"submitter_affiliation":["Human Technopole"],"submitter_country":["Italy"],"additional_accession":[]},"is_claimable":false,"name":"Insulin synthesis is sustained by readenylation of its own mRNA.","description":"Insulin is an essential regulator of glucose homeostasis in vertebrates, and impairment of its synthesis or action leads to diabetes with severe health complications in humans. It is therefore essential to understand how beta cells control insulin synthesis and secretion, including the transcription, translation and decay of its messenger RNA. Using sequencing-based poly(A) tail length profiling  from human tissue, genetic evidence for type 2 diabetes, bulk and single-cell transcriptomics and perturbation experiments, here we find that the insulin mRNA is stabilized through readenylation by noncanonical poly(A) polymerases of the TENT5 family. We show that TENT5 activity is highly specific, promoted by both localization at the endoplasmic reticulum and regulatory sequences within the insulin mRNA and stimulated by glucose. Overall, our findings provide a mechanistic link between the dynamic control of insulin production by beta cells and the direct regulation of insulin mRNA 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