Structural highlights
Function
TLBP_THET8 Part of the tripartite ATP-independent periplasmic (TRAP) transport system involved in the uptake of lactate. This protein specifically binds L-lactate.[UniProtKB:P37676][1]
Publication Abstract from PubMed
L-Lactate, traditionally considered a metabolic waste product, is increasingly recognized as an important intercellular energy currency in mammals. To enable investigations of the emerging roles of intercellular shuttling of L-lactate, we now report an intensiometric green fluorescent genetically encoded biosensor for extracellular L-lactate. This biosensor, designated eLACCO1.1, enables cellular resolution imaging of extracellular L-lactate in cultured mammalian cells and brain tissue.
A genetically encoded fluorescent biosensor for extracellular L-lactate.,Nasu Y, Murphy-Royal C, Wen Y, Haidey JN, Molina RS, Aggarwal A, Zhang S, Kamijo Y, Paquet ME, Podgorski K, Drobizhev M, Bains JS, Lemieux MJ, Gordon GR, Campbell RE Nat Commun. 2021 Dec 6;12(1):7058. doi: 10.1038/s41467-021-27332-2. PMID:34873165[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Akiyama N, Takeda K, Miki K. Crystal structure of a periplasmic substrate-binding protein in complex with calcium lactate. J Mol Biol. 2009 Sep 25;392(3):559-65. Epub 2009 Jul 22. PMID:19631222 doi:10.1016/j.jmb.2009.07.043
- ↑ Nasu Y, Murphy-Royal C, Wen Y, Haidey JN, Molina RS, Aggarwal A, Zhang S, Kamijo Y, Paquet ME, Podgorski K, Drobizhev M, Bains JS, Lemieux MJ, Gordon GR, Campbell RE. A genetically encoded fluorescent biosensor for extracellular L-lactate. Nat Commun. 2021 Dec 6;12(1):7058. PMID:34873165 doi:10.1038/s41467-021-27332-2
