Control of cystic fibrosis transmembrane conductance regulator expression by BAP31

Lambert, Georg, Becker, Bernd, Schreiber, Rainer, Boucherot, Anissa, Reth, Michael and Kunzelmann, Karl (2001) Control of cystic fibrosis transmembrane conductance regulator expression by BAP31. Journal of Biological Chemistry, 276 23: 20340-20345. doi:10.1074/jbc.M011209200

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Author Lambert, Georg
Becker, Bernd
Schreiber, Rainer
Boucherot, Anissa
Reth, Michael
Kunzelmann, Karl
Title Control of cystic fibrosis transmembrane conductance regulator expression by BAP31
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2001-06-08
Sub-type Article (original research)
DOI 10.1074/jbc.M011209200
Open Access Status File (Publisher version)
Volume 276
Issue 23
Start page 20340
End page 20345
Total pages 6
Editor Herbert Tabor
Place of publication United States
Publisher The American Society for Biochemistry and Molecular Biology
Collection year 2001
Language eng
Subject C1
270104 Membrane Biology
730110 Respiratory system and diseases (incl. asthma)
Formatted abstract
Expression of the cystic fibrosis transmembrane conductance regulator (CFTR) is stringently controlled by molecular chaperones participating in formation of the quality control system. It has been shown that about 75% of all CFTR protein and close to 100% of the [ΔPhe508] CFTR variant are rapidly degraded before leaving the endoplasmic reticulum (ER). B cell antigen receptor-associated proteins (BAPs) are ubiquitously expressed integral membrane proteins that may control association with the cytoskeleton, vesicular transport, or retrograde transport from thecis Golgi to the ER. The present study delivers evidence for cytosolic co-localization of both BAP31 and CFTR and for the control of expression of recombinant CFTR in Chinese hamster ovary (CHO) cells and Xenopus oocytes by BAP31. Antisense inhibition of BAP31 in various cell types increased expression of both wild-type CFTR and [ΔPhe508]CFTR and enabled cAMP-activated Cl− currents in [ΔPhe508]CFTR-expressing CHO cells. Coexpression of CFTR together with BAP31 attenuated cAMP-activated Cl−currents in Xenopus oocytes. These data therefore suggest association of BAP31 with CFTR that may control maturation or trafficking of CFTR and thus expression in the plasma membrane.
Keyword Biochemistry & Molecular Biology
Endoplasmic-reticulum
Delta-f508 Cftr
Chloride Channel
Retrieval Signal
Epithelial-cells
Cl Secretion
Proteins
Degradation
Maturation
Er
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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Created: Tue, 14 Aug 2007, 15:12:04 EST