ArticleAnalytical biochemistry2018
A mass spectrometry based transport assay for studying EmrE transport of unlabeled substrates.
Article in Analytical biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- Cooperative Gating of a KJournal of the American Chemical Society · 2024Article
- Highly coupled transport can be achieved in free-exchange transport models.The Journal of general physiology · 2020Article
- Inducing conformational preference of the membrane protein transporter EmrE through conservative mutations.eLife · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Membrane transporters are an important class of proteins which remain challenging to study. Transport assays are crucial to developing our understanding of such proteins as they allow direct measurement of their transport activity. However, currently available methods for monitoring liposomal loading of organic substrates primarily rely on detection of radioactively or fluorescently labeled substrates. The requirement of a labeled substrate significantly restricts the systems and substrates that can be studied. Here we present a mass spectrometry based detection method for liposomal uptake assays that eliminates the need for labeled substrates. We demonstrate the efficacy of the assay with EmrE, a small multidrug resistance transporter found in E. coli that has become a model transport system for the study of secondary active transport. Furthermore, we develop a method for differentiation between bound and transported substrate, enhancing the information gained from the liposomal uptake assay. The transport assay presented here is readily applicable to other transport systems and substrates.
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Registered trials
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