期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 25, 期 1, 页码 7-14出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzr054
关键词
CFTR; mass spectrometry; palmitoylation; post-translational modification; protein purification
资金
- Cystic Fibrosis Foundation [R464-CR07, DELUCA05XX0]
- National Institutes of Health [P30 DK072482, 1K23DK075788, 1R03DK084110]
- Genetically Defined Microbe and Expression Core of the University of Alabama at Birmingham Mucosal HIV and Immunobiology Center (NIH) [DK64400]
- National Institutes of Health/National Center for Research Resources [S10 RR019231]
- University of Alabama at Birmingham Center for Nutrient-Gene Interaction [U54 CA100949]
- Purdue-University of Alabama at Birmingham Botanicals Center for Age-Related Disease [P50AT00477]
- University of Alabama at Birmingham O'Brien Acute Kidney Injury Center [P30DK079337]
- University of Alabama at Birmingham Skin Disease Research Center [P30AR50948]
- University of Alabama at Birmingham Lung Health Center
Post-translational modifications (PTMs) play a crucial role during biogenesis of many transmembrane proteins. Previously, it had not been possible to evaluate PTMs in cystic fibrosis transmembrane conductance regulator (CFTR), the epithelial ion channel responsible for cystic fibrosis, because of difficulty obtaining sufficient amounts of purified protein. We recently used an inducible overexpression strategy to generate recombinant CFTR protein at levels suitable for purification and detailed analysis. Using liquid chromatography (LC) tandem and multiple reaction ion monitoring (MRM) mass spectrometry, we identified specific sites of PTMs, including palmitoylation, phosphorylation, methylation and possible ubiquitination. Many of these covalent CFTR modifications have not been described previously, but are likely to influence key and clinically important molecular processes including protein maturation, gating and the mechanisms underlying certain mutations associated with disease.
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