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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pillai, Meghan K. Stamnes, Susan J. Lorca, Ramón A. Wright, Michael E. England, Sarah K. Hsiao, Jordy J. |
| Description | Author Affiliation: Lorca RA ( From the Department of Obstetrics and Gynecology, Washington University in St. Louis School of Medicine, St. Louis, Missouri 63110 and.) |
| Abstract | The large-conductance Ca(2+)-activated K(+) (BK(Ca)) channel is essential for maintaining the membrane in a hyperpolarized state, thereby regulating neuronal excitability, smooth muscle contraction, and secretion. The BK(Ca) -subunit has three predicted initiation codons that generate proteins with N-terminal ends starting with the amino acid sequences MANG, MSSN, or MDAL. Because the N-terminal region and first transmembrane domain of the -subunit are required for modulation by auxiliary ß1-subunits, we examined whether ß1 differentially modulates the N-terminal BK(Ca) -subunit isoforms. In the absence of ß1, all isoforms had similar single-channel conductances and voltage-dependent activation. However, whereas ß1 did not modulate the voltage-activation curve of MSSN, ß1 induced a significant leftward shift of the voltage activation curves of both the MDAL and MANG isoforms. These shifts, of which the MDAL was larger, occurred at both 10 µM and 100 µM Ca(2+). The ß1-subunit increased the open dwell times of all three isoforms and decreased the closed dwell times of MANG and MDAL but increased the closed dwell times of MSSN. The distinct modulation of voltage activation by the ß1-subunit may be due to the differential effect of ß1 on burst duration and interburst intervals observed among these isoforms. Additionally, we observed that the related ß2-subunit induced comparable leftward shifts in the voltage-activation curves of all three isoforms, indicating that the differential modulation of these isoforms was specific to ß1. These findings suggest that the relative expression of the N-terminal isoforms can fine-tune BK(Ca) channel activity in cells, highlighting a novel mechanism of BK(Ca) channel regulation. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 14 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-04-04 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium Metabolism Large-Conductance Calcium-Activated Potassium Channel Alpha Subunits Large-Conductance Calcium-Activated Potassium Channel Beta Subunits HEK293 Cells Genetics Protein Isoforms 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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