Human ABCC1 interacts and colocalizes with ATP synthase α, revealed by interactive proteomics analysis

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Published on: April 1, 2017

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
PubMed

Insights

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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