Journal
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
Volume 311, Issue 4, Pages L719-L733Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajplung.00431.2015
Keywords
cystic fibrosis; protein trafficking; glycosylation; ubiquitination; phosphorylation; palmitoylation
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Funding
- National Institutes of Health [GM-075061, DK-079307]
- Cystic Fibrosis Foundation Therapeutics Grant [BRODSK13XX0, SORSCH13XX0]
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Posttranslational modifications add diversity to protein function. Throughout its life cycle, the cystic fibrosis transmembrane conductance regulator (CFTR) undergoes numerous covalent posttranslational modifications (PTMs), including glycosylation, ubiquitination, sumoylation, phosphorylation, and palmitoylation. These modifications regulate key steps during protein biogenesis, such as protein folding, trafficking, stability, function, and association with protein partners and therefore may serve as targets for therapeutic manipulation. More generally, an improved understanding of molecular mechanisms that underlie CFTR PTMs may suggest novel treatment strategies for CF and perhaps other protein conformational diseases. This review provides a comprehensive summary of co- and posttranslational CFTR modifications and their significance with regard to protein biogenesis.
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