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Originally published In Press as doi:10.1074/jbc.M011209200 on March 26, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20340-20345, June 8, 2001
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Control of Cystic Fibrosis Transmembrane Conductance Regulator Expression by BAP31*

Georg LambertDagger §, Bernd Becker§, Rainer Schreiber||, Anissa Boucherot||, Michael Reth**, and Karl Kunzelmann||Dagger Dagger

From the Dagger  Physiologisches Institut, Universität Zürich Irchel, CH-8057 Zürich, Switzerland, the  Uni-Klinik Regensburg, Department of Dermatology, 93052 Regensburg, Germany, the || Department of Physiology & Pharmacology, University of Queensland, St. Lucia, QLD 4072, Brisbane, Australia, and the ** Department of Molecular Immunology, Biology III, University of Freiburg, and Max-Planck-Institut für Immunobiologie, Freiburg, Germany

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 [Delta Phe508] 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 the cis 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 [Delta Phe508]CFTR and enabled cAMP-activated Cl- currents in [Delta Phe508]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.


* This work was supported by DFG Ku756/4-1, Mukoviszidose e.V., ARC -00/ARCS243, Cystic Fibrosis Australia, and DFG SFB 388.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to the present work.

Dagger Dagger To whom correspondence should be addressed. Tel.: 61 07 3365 4104; Fax: 61 07 3365 1766; E-mail: kunzelmann@plpk.uq.edu.au.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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