Lambert, Georg and Becker, Bernd and Schreiber, Rainer and Boucherot, Anissa and Reth, Michael and Kunzelmann, Karl (2001) Control of cystic fibrosis transmembrane conductance regulator expression by BAP31. JOURNAL OF BIOLOGICAL CHEMISTRY, 276 (23). pp. 20340-20345. ISSN 0021-9258
Full text not available from this repository. (Request a copy)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 [Delta Phe(508)] 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 Phe(508)]CFTR and enabled cAMP-activated CI- currents in [Delta Phe(508)]CFTR-expressing CHO cells. Coexpression of CFTR together with BAP31 attenuated cAMP-activated CI- 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ENDOPLASMIC-RETICULUM; DELTA-F508 CFTR; CHLORIDE CHANNEL; RETRIEVAL SIGNAL; EPITHELIAL-CELLS; CL SECRETION; PROTEINS; DEGRADATION; MATURATION; ER; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Dermatologie und Venerologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 17 Jan 2022 16:21 |
| Last Modified: | 17 Jan 2022 16:21 |
| URI: | https://pred.uni-regensburg.de/id/eprint/41345 |
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