Solute carrier family 7 member 5 (LAT1) (LAT1)

Solute carrier family 7 member 5 (SLC7A5), also known as L-type amino acid transporter 1 (LAT1), is a transmembrane protein that functions as a sodium-independent exchanger of large neutral amino acids, including tyrosine, leucine, and phenylalanine (NIH.gov; MDPI.com). In many malignancies, LAT1 is significantly overexpressed to support the metabolic reprogramming required for rapid cell division, where it facilitates both protein synthesis and the activation of the nutrient-sensing mTORC1 pathway (NIH.gov; ResearchGate.net). The specific uptake of tyrosine via LAT1 is widely exploited in clinical oncology for diagnostic imaging using PET tracers like 18F-FET, which provide high contrast between tumor and normal tissue (NIH.gov). Therapeutically, LAT1 is targeted by selective inhibitors such as JPH203 to induce amino acid starvation and inhibit tumor progression (NIH.gov). Furthermore, LAT1 is the primary transporter for boronophenylalanine (BPA), a key agent in boron neutron capture therapy (BNCT), enabling the selective delivery of therapeutic agents to cancer cells (NIH.gov).

Other names

L-type amino acid transporter 1SLC7A5CD98 light chain4F2 light chain4F2LC

Inhibition of the LAT1 transporter prevents the influx of essential large neutral amino acids, such as tyrosine and leucine, into the cytoplasm. This leads to intracellular amino acid starvation, which downregulates the mTORC1 pathway and induces the general amino acid control (GAAC) response, ultimately resulting in suppressed protein synthesis and tumor cell apoptosis (Kanai, 2021; NIH.gov).