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Acetylome, carbamylome, and phosphoproteome of RAW 264.7 cells treated with bacterial lipopolysaccharide

ABSTRACT: Proteome, acetylome/carbamylome, and phosphoproteome of RAW 264.7 cells treated for 24 h with bacterial lipopolysaccharide. Samples were digested with trypsin in a buffer containing urea or sodium deoxycholate, labeled with tandem mass tags, and fractionated by high pH reverse phase chromatography. Samples were sequentially enriched by IMAC and anti-acetyllysine immunoaffinity capturing before analyzing by LC-MS/MS.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Ernesto S. Nakayasu

PROVIDER: MSV000092020 | MassIVE | Tue May 23 20:50:00 BST 2023

REPOSITORIES: MassIVE

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Analysis of a macrophage carbamylated proteome reveals a function in post-translational modification crosstalk.

You Youngki Y Tsai Chia-Feng CF Patel Rishi R Sarkar Soumyadeep S Clair Geremy G Zhou Mowei M Liu Tao T Metz Thomas O TO Das Chittaranjan C Nakayasu Ernesto S ES

Cell communication and signaling : CCS 20230918 1

<h4>Background</h4>Lysine carbamylation is a biomarker of rheumatoid arthritis and kidney diseases. However, its cellular function is understudied due to the lack of tools for systematic analysis of this post-translational modification (PTM).<h4>Methods</h4>We adapted a method to analyze carbamylated peptides by co-affinity purification with acetylated peptides based on the cross-reactivity of anti-acetyllysine antibodies. We also performed immobilized-metal affinity chromatography to enrich for ...[more]

PMID: 37723562

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Acetylome dynamics during differentiation of SGBS adipocytes

Project description:Here, we identified temporal dynamics of the acetylome during adipocyte differentiation in human SGBS cells, applying untargeted proteomics in combination with immunoaffinity purification of acetylated peptides. Samples were taken at initiation of differentiation, at an intermediate and terminal time point.

2024-06-13 | PXD045768 | Pride

Acetylome dynamics during differentiation of 3T3-L1 adipocytes

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Workflow enabling deepscale immunopeptidome, proteome, ubiquitylome, phosphoproteome, and acetylome analyses of sample-limited tissues.

Project description:Serial multi-omic analysis of proteome, phosphoproteome, and acetylome provides insights into changes in protein expression, cell signaling, cross-talk and epigenetic pathways involved in disease pathology and treatment. However, ubiquitylome and HLA peptidome data collection used to understand protein degradation and antigen presentation have not together been serialized, and instead require separate samples for parallel processing using distinct protocols. Here we present MONTE, a highly sensitive multi-omic native tissue enrichment workflow, that enables serial, deep-scale analysis of HLA-I and HLA-II immunopeptidome, ubiquitylome, proteome, phosphoproteome, and acetylome from the same tissue sample. We demonstrate that the depth of coverage and quantitative precision of each 'ome is not compromised by serialization, and the addition of HLA immunopeptidomics enables the identification of peptides derived from cancer/testis antigens and patient specific neoantigens. We evaluate the technical feasibility of the MONTE workflow using a small cohort of patient lung adenocarcinoma tumors.

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Proteomic determination of the lysine acetylome and phosphoproteome in the rat native inner medullary collecting duct.

Project description:Phosphorylation and lysine (K)-acetylation are dynamic posttranslational modifications of proteins. Previous proteomic studies have identified over 170,000 phosphorylation sites and 15,000 K-acetylation sites in mammals. We recently reported that the inner medullary collecting duct (IMCD), which functions in the regulation of water-reabsorption, via the actions of vasopressin, expresses many of the enzymes that can modulated K-acetylation. The purpose of this study was to determine the K-acetylated or phosphorylated proteins expressed in IMCD cells. Second we questioned whether vasopressin V2 receptor activation significantly affects the IMCD acetylome or phosphoproteome? K-acetylated or serine-, threonine-, or tyrosine-phosphorylated peptides were identified from native rat IMCDs by proteomic analysis with four different enzymes (trypsin, chymotrypsin, ASP-N, or Glu-C) to generate a high-resolution proteome. K-acetylation was identified in 431 unique proteins, and 64% of the K-acetylated sites were novel. The acetylated proteins were expressed in all compartments of the cell and were enriched in pathways including glycolysis and vasopressin-regulated water reabsorption. In the vasopressin-regulated water reabsorption pathway, eight proteins were acetylated, including the novel identification of the basolateral water channel, AQP3, acetylated at K282; 215 proteins were phosphorylated in this IMCD cohort, including AQP2 peptides that were phosphorylated at four serines: 256, 261, 264, and 269. Acute dDAVP did not significantly affect the IMCD acetylome; however, it did significantly affect previously known vasopressin-regulated phosphorylation sites. In conclusion, presence of K-acetylated proteins involved in metabolism, ion, and water transport in the IMCD points to multiple roles of K-acetylation beyond its canonical role in transcriptional regulation.

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Suberoylanilide Hydroxamic Acid (SAHA) Treatment Reveals Crosstalk Among Proteome, Phosphoproteome, and Acetylome in Nasopharyngeal Carcinoma Cells.

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Profiling of mouse brain acetylome and proteome

Project description:Nε-Lysine acetylation is a reversible post-translational protein modification (PTM). In recent years, genetic analysis and animal model studies have shown that protein acetylation is closely related to the development of the nervous system and neurodegenerative diseases such as PD and AD. Here, we aim to profile the mouse brain acetylome by using FSAP, immunoaffinity precipitation of acetylpeptides and mass spectrometry method. We identified 1,591 acetylated proteins containing 4,182 acetylation modification sites in C57BL/6 mice brain. These proteins were involved in myelin sheath, mitochondrial inner membrane and neuron synapse. While KEGG enrichment analysis indicated that these proteins are associated with neurological diseases, such as Alzheimer's disease and Huntington disease. Taken together, we provided a comprehensive profile and clues for understanding the role of acetylated proteins in neuropathology such as neurogenesis, degeneration and aging.

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Profiling of mouse brain acetylome and proteome

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Transcriptome and acetylome profiling identify crucial steps of neuronal differentiation in Rubinstein-Taybi syndrome

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