Human ABCC1 interacts and colocalizes with ATP synthase α, revealed by interactive proteomics analysis
| Autor: | Wei Mo, Petra Hrncirova, Milos V. Novotny, Randy J. Arnold, Zhaomin Li, Raghuram Ambadipudi, Jian Ting Zhang, Youyun Yang, Elias Georges |
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| Rok vydání: | 2011 |
| Předmět: |
Proteomics
Molecular Sequence Data ATP-binding cassette transporter Biology Biochemistry Models Biological Article ATP synthase gamma subunit Protein Interaction Mapping V-ATPase Humans Immunoprecipitation Amino Acid Sequence Binding site Phosphorylation Protein kinase A Binding Sites ATP synthase Reproducibility of Results General Chemistry Mitochondrial Proton-Translocating ATPases HEK293 Cells biology.protein Multidrug Resistance-Associated Proteins ATP synthase alpha/beta subunits Protein Binding |
| Zdroj: | J Proteome Res |
| ISSN: | 1535-3907 |
| Popis: | Human ABCC1 is a member of the ATP-binding cassette (ABC) transporter superfamily, and its overexpression has been shown to cause multidrug resistance by active efflux of a wide variety of anticancer drugs. ABCC1 has been shown to exist and possibly function as a homodimer. However, a possible heterocomplex involving ABCC1 has been indicated. In this study, we performed an interactive proteomics study to examine proteins that bind to and form heterocomplexes with ABCC1 using coimmunoprecipitation and tandem mass spectrometry (MS/MS) analyses. We found that ATP synthase α binds to ABCC1 in plasma membranes with a ratio of 2:1. The ATP synthase α binding site in ABCC1 is located in the linker domain at the carboxyl core of ABCC1, and phosphorylation of the linker domain at the protein kinase A site enhances ATP synthase α binding. The interaction between ABCC1 and ATP synthase α in a heterocomplex may indicate a novel function of ABCC1 in regulating extracellular ATP level and purinergic signaling cascade. |
| Databáze: | OpenAIRE |
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