A mutation in the beta interaction domain of the Ca(2+) channel alpha(1C) subunit reduces the affinity of the (+)-[(3)H]isradipine binding site
| Autor: | Monika Hitzl, Jörg Striessnig, Birgit Neuhuber, Bernhard E. Flucher |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Immunoprecipitation
Protein subunit Immunofluorescence Biophysics medicine.disease_cause Tritium Biochemistry Cell Line Radioligand Assay Radioligand binding Structural Biology Genetics medicine Binding site Molecular Biology DNA Primers (+)-[3H]Isradipine Mutation Isradipine Binding Sites Base Sequence Effector Chemistry Calcium channel Cell Biology Calcium Channel Blockers Precipitin Tests Cell culture Calcium Channels medicine.drug |
| Zdroj: | FEBS letters. 524(1-3) |
| ISSN: | 0014-5793 |
| Popis: | The molecular mechanisms of how alpha(1) and beta subunits of voltage-gated Ca(2+) channels interact with one another are still controversial. Here we show that despite a mutation in the beta interaction domain that has previously been shown to disrupt binding, alpha(1C)Y467S and beta(1a-myc) still formed immunoprecipitable complexes when coexpressed in tsA201 cells. However, the alpha(1C)Y467S-beta(1a-myc) complexes had a decreased affinity to (+)-[(3)H]isradipine. This indicates that the beta interaction domain in the I-II loop of the alpha(1) subunit is not merely an anchor required for the functional interaction of the two Ca(2+) channel subunits but is itself part of the effector pathway for beta-induced channel modulation. |
| Databáze: | OpenAIRE |
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