Analysis of conventional and unconventional trafficking of CFTR and other membrane proteins

Heon Yung Gee, Joo Young Kim, Min Goo Lee

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


The cystic fibrosis transmembrane conductance regulator (CFTR) is a polytopic transmembrane protein that functions as a cAMP-activated anion channel at the apical membrane of epithelial cells. Mutations in CFTR cause cystic fibrosis and are also associated with monosymptomatic diseases in the lung, pancreas, intestines, and vas deferens. Many disease-causing CFTR mutations, including the deletion of a single phenylalanine residue at position 508 (ΔF508-CFTR), result in protein misfolding and trafficking defects. Therefore, intracellular trafficking of wild-type and mutant CFTR has been studied extensively, and results from these studies significantly contribute to our general understanding of mechanisms involved in the cell-surface trafficking of membrane proteins. CFTR is a glycoprotein that undergoes complex N-glycosylation as it passes through Golgi-mediated conventional exocytosis. Interestingly, results from recent studies revealed that CFTR and other membrane proteins can reach the plasma membrane via an unconventional alternative route that bypasses Golgi in specific cellular conditions. Here, we describe methods that have been used to investigate the conventional and unconventional surface trafficking of CFTR. With appropriate modifications, the protocols described in this chapter can also be applied to studies investigating the intracellular trafficking of other plasma membrane proteins.

Original languageEnglish
Pages (from-to)137-154
Number of pages18
JournalMethods in Molecular Biology
Publication statusPublished - 2015

Bibliographical note

Publisher Copyright:
© Springer Science+Business Media New York 2015.

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics


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