Quantitative proteomics identifies Gemin5, a scaffolding protein involved in ribonucleoprotein assembly, as a novel partner for eukaryotic initiation factor 4E.

Journal article

Protein complexes are dynamic entities; identification and quantitation of their components is critical in elucidating functional roles under specific cellular conditions. We report the first quantitative proteomic analysis of the human cap-binding protein complex. Components and proteins associated with the translation initiation eIF4F complex that may affect complex formation were identified and quantitated under distinct growth conditions. Site-specific phosphorylation of eIF4E and eIF4G a...

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Authors: Fierro-Monti, I; Mohammed, S; Matthiesen, R; Santoro, R; Burns, J

• Publication status: Published
• Journal: Journal of proteome research
• Volume: 5
• Issue: 6
• Pages: 1367-1378
• Publication date: 2006-06-01
• DOI: 10.1021/pr0504539
• EISSN: 1535-3907
• ISSN: 1535-3893
• Language: English
• Keywords: RNA Caps; Amino Acid Sequence; Humans; Molecular Sequence Data; Ribonucleoproteins, Small Nuclear; Phosphorylation; RNA Stability; Mutagenesis, Site-Directed; Eukaryotic Initiation Factor-4E; Protein Binding; Mass Spectrometry; Base Sequence; Eukaryotic Initiation Factor-4G; Cell Line