Proteomic snapshot of the EGF‐induced ubiquitin network

• Published in: Molecular systems biology Vol. 7; no. 1; pp. 462 - n/a
• Main Authors: Argenzio, Elisabetta, Bange, Tanja, Oldrini, Barbara, Bianchi, Fabrizio, Peesari, Raghunath, Mari, Sara, Di Fiore, Pier Paolo, Mann, Matthias, Polo, Simona
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 2011; John Wiley & Sons, Ltd; EMBO Press; Nature Publishing Group; Springer Nature
• Subjects: Actin; Amino acids; Animals; Blotting, Western; Cancer; Cascades; Cell adhesion; Cell adhesion & migration; Cell culture; Cell Line; Chains; Cluster Analysis; Conjugation; Crosstalk; Deoxyribonucleic acid; DNA; DNA damage; EMBO31; EMBO37; Endocytosis; Enrichment; Enzymes; EphA2 protein; Epidermal growth factor; Epidermal Growth Factor - chemistry; Epidermal Growth Factor - metabolism; Epidermal growth factor receptors; HeLa Cells; Homeostasis; Humans; Internalization; Intracellular; Intracellular signalling; Kinases; Localization; Mass Spectrometry; Mass spectroscopy; Mice; Microscopy, Fluorescence; Molecular chains; Monomers; Network analysis; Networks; Phosphorylation; Phosphotyrosine; Physiology; Protein purification; Protein-tyrosine kinase; Protein-tyrosine kinase receptors; Proteins; Proteome - chemistry; Proteome - metabolism; Proteomics - methods; Purification; Receptor, EphA2 - metabolism; Screens; Signal Transduction; Stimulation; Systems Biology - methods; Transcription; Translation; Tyrosine; Ubiquitin - chemistry; Ubiquitin - metabolism

The activity, localization and fate of many cellular proteins are regulated through ubiquitination, a process whereby one or more ubiquitin (Ub) monomers or chains are covalently attached to target proteins. While Ub‐conjugated and Ub‐associated proteomes have been described, we lack a high‐resoluti...