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Human ABCC1 interacts and colocalizes with ATP synthase α, revealed by interactive proteomics analysis
Youyun Yang1, Zhaomin Li, Wei Mo
1Department of Pharmacology and Toxicology and IU Simon Cancer Center, Indiana University School of Medicine , Indianapolis, Indiana 46202, United States.
Journal of Proteome Research
|December 23, 2011
Summary
The ATP-binding cassette (ABC) transporter ABCC1 interacts with ATP synthase alpha in human cells. This novel heterocomplex may regulate extracellular ATP levels and purinergic signaling.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Human ABCC1, an ATP-binding cassette transporter, is implicated in multidrug resistance via anticancer drug efflux.
- ABCC1 is known to function as a homodimer, but evidence suggests potential heterocomplex formation.
Purpose of the Study:
- To identify proteins interacting with ABCC1 and forming heterocomplexes.
- To elucidate the functional implications of ABCC1 heterocomplex formation.
Main Methods:
- Interactive proteomics using coimmunoprecipitation.
- Tandem mass spectrometry (MS/MS) analyses to identify binding partners.
Main Results:
- ATP synthase alpha was identified as a binding partner of ABCC1 in plasma membranes at a 2:1 ratio.
- The binding site for ATP synthase alpha on ABCC1 is in the linker domain, and phosphorylation enhances this interaction.
- A novel heterocomplex between ABCC1 and ATP synthase alpha was discovered.
Conclusions:
- The interaction between ABCC1 and ATP synthase alpha suggests a new role for ABCC1.
- This heterocomplex may regulate extracellular ATP levels.
- ABCC1 might play a role in the purinergic signaling cascade.
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