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Mechanistic basis of L-lactate transport in the SLC16 solute carrier family

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Bosshart Patrick D., Kalbermatter David, Bonetti Sara, Fotiadis Dimitrios,
Project Structure and supramolecular organization of membrane transport proteins
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Original article (peer-reviewed)

Journal Nature Communications
Volume (Issue) 10(1)
Page(s) 2649 - 2649
Title of proceedings Nature Communications
DOI 10.1038/s41467-019-10566-6

Open Access

URL http://doi.org/10.1038/s41467-019-10566-6
Type of Open Access Publisher (Gold Open Access)

Abstract

In human and other mammalian cells, transport of L-lactate across plasma membranes is mainly catalyzed by monocarboxylate transporters (MCTs) of the SLC16 solute carrier family. MCTs play an important role in cancer metabolism and are promising targets for tumor treatment. Here, we report the crystal structures of an SLC16 family homologue with two different bound ligands at 2.54 and 2.69 Å resolution. The structures show the transporter in the pharmacologically relevant outward-open conformation. Structural information together with a detailed structure-based analysis of the transport function provide important insights into the molecular working mechanisms of ligand binding and L-lactate transport.
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