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Published 11 October 2004. doi:10.1083/jcb.200401035
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 1, 65-74
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Article

 COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code

Xiaodong Wang1, Jeanne Matteson1, Yu An1,2, Bryan Moyer1, Jin-San Yoo1, Sergei Bannykh1, Ian A. Wilson2, John R. Riordan4, and William E. Balch1,3

1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
2 Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037
3 The Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, CA 92037
4 Mayo Foundation and S.C. Johnson Medical Research Center, Mayo Clinic, Scottsdale, AZ 85259

Correspondence to W.E. Balch: webalch{at}scripps.edu

Cystic fibrosis (CF) is a childhood hereditary disease in which the most common mutant form of the CF transmembrane conductance regulator (CFTR) {Delta}F508 fails to exit the endoplasmic reticulum (ER). Export of wild-type CFTR from the ER requires the coat complex II (COPII) machinery, as it is sensitive to Sar1 mutants that disrupt normal coat assembly and disassembly. In contrast, COPII is not used to deliver CFTR to ER-associated degradation. We find that exit of wild-type CFTR from the ER is blocked by mutation of a consensus di-acidic ER exit motif present in the first nucleotide binding domain. Mutation of the code disrupts interaction with the COPII coat selection complex Sec23/Sec24. We propose that the di-acidic exit code plays a key role in linking CFTR to the COPII coat machinery and is the primary defect responsible for CF in {Delta}F508-expressing patients.

X. Wang and J. Matteson contributed equally to this paper.

Abbreviations used in this paper: BFA, brefeldin A; BHK, baby hamster kidney; CF, cystic fibrosis; CFTR, CF transmembrane conductance regulator; COPII, coat complex II; endo H, endoglycosidase H; ERAD, ER-associated degradation; GAP, guanine nucleotide activating protein; NBD1, nucleotide binding domain 1; VSV-G, vesicular stomatitis virus glycoprotein.


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