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Am J Physiol Lung Cell Mol Physiol. 2016 Oct 1;311(4):L719-L733. doi: 10.1152/ajplung.00431.2015. Epub 2016 Jul 29.

Trafficking and function of the cystic fibrosis transmembrane conductance regulator: a complex network of posttranslational modifications.

Author information

1
Cystic Fibrosis Research Center, University of Alabama at Birmingham, Birmingham, Alabama.
2
Department of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, Alabama.
3
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania; and.
4
Department of Pediatrics, Emory University, Atlanta, Georgia esorscher@emory.edu.

Abstract

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.

KEYWORDS:

cystic fibrosis; glycosylation; palmitoylation; phosphorylation; protein trafficking; ubiquitination

PMID:
27474090
PMCID:
PMC5142128
DOI:
10.1152/ajplung.00431.2015
[Indexed for MEDLINE]
Free PMC Article

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