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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | González, Carlos Torres, Yolima P. Pupo, Amaury Contreras, Gustavo F. Neely, Alan Castillo, Karen Latorre, Ramon |
| Description | Author Affiliation: Castillo K ( Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso 2366103, Chile); Contreras GF ( Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso 2366103, Chile); Pupo A ( Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso 2366103, Chile); Torres YP ( Departmento de Nutricion y Bioquimica, Facultad de Ciencias, Pontificia Universidad Javeriana, Bogota DC 110111, Colombia.); Neely A ( Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso 2366103, Chile); González C ( Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso 2366103, Chile); Latorre R ( Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso 2366103, Chile); |
| Abstract | Being activated by depolarizing voltages and increases in cytoplasmic Ca(2+), voltage- and calcium-activated potassium (BK) channels and their modulatory ß-subunits are able to dampen or stop excitatory stimuli in a wide range of cellular types, including both neuronal and nonneuronal tissues. Minimal alterations in BK channel function may contribute to the pathophysiology of several diseases, including hypertension, asthma, cancer, epilepsy, and diabetes. Several gating processes, allosterically coupled to each other, control BK channel activity and are potential targets for regulation by auxiliary ß-subunits that are expressed together with the (BK)-subunit in almost every tissue type where they are found. By measuring gating currents in BK channels coexpressed with chimeras between ß1 and ß3 or ß2 auxiliary subunits, we were able to identify that the cytoplasmic regions of ß1 are responsible for the modulation of the voltage sensors. In addition, we narrowed down the structural determinants to the N terminus of ß1, which contains two lysine residues (i.e., K3 and K4), which upon substitution virtually abolished the effects of ß1 on charge movement. The mechanism by which K3 and K4 stabilize the voltage sensor is not electrostatic but specific, and the (BK)-residues involved remain to be identified. This is the first report, to our knowledge, where the regulatory effects of the ß1-subunit have been clearly assigned to a particular segment, with two pivotal amino acids being responsible for this modulation. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 15 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium Metabolism Ion Channel Gating Physiology Large-Conductance Calcium-Activated Potassium Channel Beta Subunits Potassium Animals Binding Sites Genetics Chemistry Lysine Membrane Potentials Models, Molecular Mutation Oocytes Protein Structure, Tertiary Protein Subunits Recombinant Fusion Proteins Xenopus Laevis Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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