ArticlePloS one2011
Dimerization of ABCG2 analysed by bimolecular fluorescence complementation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Disruption of the Unique ABCG-Family NBD:NBD Interface Impacts Both Drug Transport and ATP Hydrolysis.International journal of molecular sciences · 2020Article
- Development of precision medicine approaches based on inter-individual variability of BCRP/Acta pharmaceutica Sinica. B · 2019Review
- ABCI3 Is a New Mitochondrial ABC Transporter from Leishmania major Involved in Susceptibility to Antimonials and Infectivity.Antimicrobial agents and chemotherapy · 2017Article
- Defining the molecular basis of interaction between R3 receptor-type protein tyrosine phosphatases and VE-cadherin.PloS one · 2017Article
- The multidrug transporter ABCG2: still more questions than answers.Biochemical Society transactions · 2016Review
- Identification of residues in ABCG2 affecting protein trafficking and drug transport, using co-evolutionary analysis of ABCG sequences.Bioscience reports · 2015Article
- Heterodimerization, altered subcellular localization, and function of multiple zinc transporters in viable cells using bimolecular fluorescence complementation.The Journal of biological chemistry · 2015Article
- Role of the breast cancer resistance protein (BCRP/ABCG2) in drug transport--an update.The AAPS journal · 2015Review
- In situ dimerization of multiple wild type and mutant zinc transporters in live cells using bimolecular fluorescence complementation.The Journal of biological chemistry · 2014Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
ABCG2 is one of three human ATP binding cassette transporters that are functionally capable of exporting a diverse range of substrates from cells. The physiological consequence of ABCG2 multidrug transport activity in leukaemia, and some solid tumours is the acquisition of cancer multidrug resistance. ABCG2 has a primary structure that infers that a minimal functional transporting unit would be a homodimer. Here we investigated the ability of a bimolecular fluorescence complementation approach to examine ABCG2 dimers, and to probe the role of individual amino acid substitutions in dimer formation. ABCG2 was tagged with fragments of venus fluorescent protein (vYFP), and this tagging did not perturb trafficking or function. Co-expression of two proteins bearing N-terminal and C-terminal fragments of YFP resulted in their association and detection of dimerization by fluorescence microscopy and flow cytometry. Point mutations in ABCG2 which may affect dimer formation were examined for alterations in the magnitude of fluorescence complementation signal. Bimolecular fluorescence complementation (BiFC) demonstrated specific ABCG2 dimer formation, but no changes in dimer formation, resulting from single amino acid substitutions, were detected by BiFC analysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.