Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 611-616 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 277 |
| Issue number | 3 |
| DOIs | |
| State | Published - Nov 2 2000 |
Bibliographical note
Funding 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.
Funding
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.
| Funders | Funder number |
|---|---|
| National Institutes of Health (NIH) | R37-23306 |
Keywords
- L-type calcium channel
- Membrane targeting
- Protein-protein interaction
- Vacuolar H-ATPase G subunit
- Yeast two-hybrid screening
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology