The class C L-type calcium (Ca2+) channels have been implicated in many important physiological processes. Here, we have identified a mouse vacuolar H+-ATPase (V-ATPase) G2 subunit protein that bound to the C-terminal domain of the pore-forming α(1C) subunit using a yeast two-hybrid screen. Protein-protein interaction between the V-ATPase G subunit and the α(1C) subunit was confirmed using in vitro GST pull-down assays and coimmunoprecipitation from intact cells. Moreover, treatment of cells expressing L-type Ca2+ channels with a specific inhibitor of the V-ATPase blocked proper targeting of the channels to the plasma membrane. (C) 2000 Academic Press.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Nov 2 2000|
Bibliographical noteFunding Information:
This work was supported by NIH Grant R37-23306 to M.M.H. We thank Dr. Heidi Hamm and E. J. Dell for their help with yeast two-hybrid screening.
- L-type calcium channel
- Membrane targeting
- Protein-protein interaction
- Vacuolar H-ATPase G subunit
- Yeast two-hybrid screening
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology