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

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dc.contributor.author김주영-
dc.contributor.author이민구-
dc.contributor.author지헌영-
dc.date.accessioned2018-01-23T05:50:12Z-
dc.date.available2018-01-23T05:50:12Z-
dc.date.issued2015-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/155697-
dc.description.abstractThe 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.-
dc.description.statementOfResponsibilityrestriction-
dc.relation.isPartOfMethods in Molecular Biology (Clifton, N.J.)-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleAnalysis of conventional and unconventional trafficking of CFTR and other membrane proteins-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Pharmacology-
dc.contributor.googleauthorHeon Yung Gee-
dc.contributor.googleauthorJoo Young Kim-
dc.contributor.googleauthorMin Goo Lee-
dc.identifier.doi10.1007/978-1-4939-2309-0_11-
dc.contributor.localIdA00942-
dc.contributor.localIdA02781-
dc.contributor.localIdA03971-
dc.relation.journalcodeJ02226-
dc.identifier.pmid25702115-
dc.identifier.urlhttp://link.springer.com/protocol/10.1007%2F978-1-4939-2309-0_11-
dc.contributor.alternativeNameKim, Joo Young-
dc.contributor.alternativeNameLee, Min Goo-
dc.contributor.alternativeNameGee, Heon Yung-
dc.contributor.affiliatedAuthorKim, Joo Young-
dc.contributor.affiliatedAuthorLee, Min Goo-
dc.contributor.affiliatedAuthorGee, Heon Yung-
dc.citation.volume1270-
dc.citation.startPage137-
dc.citation.endPage154-
dc.identifier.bibliographicCitationMethods in Molecular Biology (Clifton, N.J.), Vol.1270 : 137-154, 2015-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers

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