Sodium-coupled neutral amino acid transporter 2 (SLC38A2)

Sodium-coupled neutral amino acid transporter 2 (SLC38A2), also known as SNAT2, is a **membrane transporter protein** that belongs to the solute carrier family 38. It is predominantly responsible for the **sodium-dependent uptake of small and medium-sized neutral amino acids** such as alanine, asparagine, cysteine, glutamine, glycine, histidine, methionine, proline, and serine[1][2][4]. SLC38A2 is expressed in a broad range of tissues, including the brain, liver, muscle, and kidney, and is adaptive to nutrient deprivation or hyperosmotic stress by increasing its expression and function. It plays critical roles in the **regulation of cell volume, cell growth, differentiation via mTORC1 signaling, and the glutamate-glutamine cycle** crucial for neurotransmission and metabolism[2][4]. In pathology, SLC38A2 is upregulated in various cancers to support enhanced amino acid uptake/glutaminolysis and has been implicated in metabolic diseases such as type 2 diabetes[3]. Its activity is modulated by available sodium and substrate amino acids, as well as hormonal and stress-related cues, making it a possible **therapeutic target for cancer and metabolic disorders**, though no direct drugs are currently used clinically[1][2][3][4].

Other names

Amino acid transporter A2SNAT2ATA2SAT2KIAA1382Protein 40-9-1System A amino acid transporter 2System A transporter 1System N amino acid transporter 2Solute carrier family 38 member 2

Drugs or ligands (such as MeAIB) act as competitive substrates or inhibitors of sodium-coupled amino acid transport, reducing or modulating uptake of neutral amino acids[2][3].