Bibliographic Details
| Title: |
A mutation in the β interaction domain of the Ca2+ channel α1C subunit reduces the affinity of the (+)-[3H]isradipine binding site |
| Authors: |
Hitzl, Monika, Striessnig, Jörg, Neuhuber, Birgit, Flucher, Bernhard E. bernhard.e.flucher@uibk.ac.at |
| Source: |
FEBS Letters. Jul2002, Vol. 524 Issue 1-3, p188. 5p. |
| Subjects: |
Calcium channels, Radioligand assay |
| Abstract: |
The molecular mechanisms of how α1 and β subunits of voltage-gated Ca2+ channels interact with one another are still controversial. Here we show that despite a mutation in the β interaction domain that has previously been shown to disrupt binding, α1CY467S and β1a-myc still formed immunoprecipitable complexes when coexpressed in tsA201 cells. However, the α1CY467S–β1a-myc complexes had a decreased affinity to (+)-[3H]isradipine. This indicates that the β interaction domain in the I–II loop of the α1 subunit is not merely an anchor required for the functional interaction of the two Ca2+ channel subunits but is itself part of the effector pathway for β-induced channel modulation. [Copyright &y& Elsevier] |
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| Database: |
Engineering Source |
