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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Azimov, Rustam Kurtz, Ira Newman, Debra Zhu, Quansheng Abuladze, Natalia Kao, Liyo |
| Description | Author Affiliation: Zhu Q ( From the Department of Medicine and quzhu@mednet.ucla.edu.); Kao L ( From the Department of Medicine and.); Azimov R ( From the Department of Medicine and.); Abuladze N ( From the Department of Medicine and.); Newman D ( From the Department of Medicine and.); Kurtz I ( From the Department of Medicine and Brain Research Institute, David Geffen School of Medicine, UCLA, Los Angeles, California 90095-1689.) |
| Abstract | The extracellular loop 3 (EL-3) of SLC4 Na(+)-coupled transporters contains 4 highly conserved cysteines and multiple N-glycosylation consensus sites. In the electrogenic Na(+)-HCO3(-) cotransporter NBCe1-A, EL-3 is the largest extracellular loop and is predicted to consist of 82 amino acids. To determine the structural-functional importance of the conserved cysteines and the N-glycosylation sites in NBCe1-A EL-3, we analyzed the potential interplay between EL-3 disulfide bonding and N-glycosylation and their roles in EL-3 topological folding. Our results demonstrate that the 4 highly conserved cysteines form two intramolecular disulfide bonds, Cys(583)-Cys(585) and Cys(617)-Cys(642), respectively, that constrain EL-3 in a folded conformation. The formation of the second disulfide bond is spontaneous and unaffected by the N-glycosylation state of EL-3 or the first disulfide bond, whereas formation of the first disulfide bond relies on the presence of the second disulfide bond and is affected by N-glycosylation. Importantly, EL-3 from each monomer is adjacently located at the NBCe1-A dimeric interface. When the two disulfide bonds are missing, EL-3 adopts an extended conformation highly accessible to protease digestion. This unique adjacent parallel location of two symmetrically folded EL-3 loops from each monomer resembles a domain-like structure that is potentially important for NBCe1-A function in vivo. Moreover, the formation of this unique structure is critically dependent on the finely tuned interplay between disulfide bonding and N-glycosylation in the membrane processed NBCe1-A dimer. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 9 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-02-27 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cysteine Chemistry Disulfides Protein Folding Sodium-Bicarbonate Symporters Amino Acid Sequence Binding Sites Genetics Metabolism Glycosylation HEK293 Cells Immunoblotting Ion Transport Microscopy, Fluorescence Molecular Sequence Data Mutation Protein Multimerization Protein Structure, Secondary Sequence Homology, Amino Acid Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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