Andrew J. Davies

TL;DR: It is concluded that MCT4, like other glycolytic enzymes, is up-regulated by hypoxia through a HIF-1α-mediated mechanism, which allows the increased lactic acid produced during Hypoxia to be rapidly lost from the cell.

TL;DR: It is demonstrated by site-directed mutagenesis that removal of all accessible cysteine residues on MCT4 does not prevent this inhibition by pCMBS, and ancillary proteins are required to maintain the catalytic activity of MCTs as well as for their translocation to the plasma membrane.

TL;DR: Measurement of the inhibitor sensitivity of several chimaeric transporters combining different domains of MCT1 and MCT4 revealed that the binding site for AR-C155858 is contained within the C-terminal half of M CT1, and involves TM (transmembrane) domains 7–10, consistent with previous data identifying Phe360 and Asp302 plus Arg306 as key residues in substrate binding and translocation by MCT 1.

TL;DR: Evidence is provided that this list of molecules identified so far must now be extended to comprise an organic molecule transporter: the monocarboxylate transporter MCT2, which may allow an influx of lactate derived from perisynaptic glial processes.

TL;DR: GATA-6 function in the cell is controlled by a complex interplay of transcriptional and translational regulation, and two alternative promoters and 5′ noncoding exons are utilized.