ArticleJournal of bioenergetics and biomembranes2011
The nucleotide-binding domain 2 of the human transporter protein MRP6.
Article in Journal of bioenergetics and biomembranes, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- The Expression Level of ABCC6 Transporter in Colon Cancer Cells Correlates with the Activation of Different Intracellular Signaling Pathways.Pathophysiology : the official journal of the International Society for Pathophysiology · 2022Article
- Structural and Functional Characterization of the ABCC6 Transporter in Hepatic Cells: Role on PXE, Cancer Therapy and Drug Resistance.International journal of molecular sciences · 2021Review
- Article
- Human bile acid transporter ASBT (SLC10A2) forms functional non-covalent homodimers and higher order oligomers.Biochimica et biophysica acta. Biomembranes · 2018Article
- Expression of some ATP-binding cassette transporters in acute myeloid leukemia.Hematology reports · 2017Article
- Mutation spectrum in the ABCC6 gene and genotype-phenotype correlations in a French cohort with pseudoxanthoma elasticum.Genetics in medicine : official journal of the American College of Medical Genetics · 2017Article
- Article
- New insights into the roles of the N-terminal region of the ABCC6 transporter.Journal of bioenergetics and biomembranes · 2016Article
- UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP.Biochemical pharmacology · 2015Article
- Multidrug Resistance Proteins (MRPs) and Cancer Therapy.The AAPS journal · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug-resistance-associated protein 6 (MRP6/ABCC6) belongs to the ABC transporter family, whose members share many characteristic features including membrane domains and two nucleotide-binding domains (NBD1 and NBD2). These function cooperatively to bind and hydrolyze ATP for the transport of substrates across biological membranes. In this study, MRP6-NBD2 (residues 1252-1503) was expressed in Escherichia coli, purified and structurally and functionally characterized. CD spectra suggested that the protein is folded. Furthermore, NBD2 is shown to be biologically active as it binds ATP and presents ATPase activity although significantly lower compared with isolated NBD1. The mixture of NBD2 and NBD1 exhibited an activity similar to the NBD2 alone, indicating that NBD1 and NBD2 form a heterodimer with the latter limiting ATP hydrolysis. These findings suggest that NBD1 has a higher tendency to form an active homodimer, which is also supported by in silico analysis of energy-minimized dimers of the homology models of the two domains.
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