Introduction of SLC7A3
SLC7A3 (solute carrier family 7 member 3) also known as CAT-3 or ATRC3, is encoded by the gene SLC7A3. SLC7A3 is a member of SLC7 family which can be divided into two major subgroups, cationic amino acid transporters (CATs, SLC7A1-4) and glycoprotein-associated amino acid transporters (gpaATs, SLC7A5-11), also called catalytic chains of the hetero(di)meric amino acid transporters (HATs). Belonging to CATs subgroup, SLC7A3 plays an important role in the transduction of L-type cationic amino acids arginine, lysine and ornithine with sodium-independent manner in various cells. The SLC7A3 gene containing 12 exons is mapped to chromosome Xq13.1. There are 2 transcript variants in this gene and they can encode different isoforms correspondingly. The topology structure of SLC7A3 is predicted to have 14 transmembrane (TM) segments and intracellular N-and C-termini. It is documented that one N-linked glycosylation site of SLC7A3 is located at the third extracellular loop, which also serves as a binding site for ecotropic murine leukemia viruses.
|Basic Information of SLC7A3|
|Protein Name||Cationic amino acid transporter 3|
|Organism||Homo sapiens (Human)|
Function of SLC7A3 Membrane Protein
The most well-known role of SLC7A3 is acting as a cationic amino acid transporter to transport arginine, which is essential for protein synthesis and production of nitric oxide (NO) and polyamines. Under certain conditions, lysine and arginine are derived exclusively from the degradation of ingested nutrients, so the uptake of L-type cationic amino acids (arginine, ornithine, and lysine) into the cells conducted by SLC7A3 transporter is extraordinarily crucial. With selective expression in brain, SLC7A3 together with SLC7A1 mediates activation of NMDA receptor and regulates the mammalian target of rapamycin (mTOR) signaling pathway, which has a central role in neuronal development and plasticity through arginine availability. It is reported that SLC7A3 can also act as an ecotropic retroviral leukemia receptor. Furthermore, SLC7A3 is upregulated in the placental chorion and therefore recognized as an excellent candidate gene for placental transport of glucose and arginine to support growth and development of the porcine conceptus during pregnancy. Rare hypomorphic variants of SLC7A3 contribute to the etiology of autism spectrum disorder (ASD).
Fig.1 The consequences of SLC7A3 dysfunction on the mTOR and NO pathways. (Nava, 2015)
Application of SLC7A3 Membrane Protein in Literature
The authors identified four rare missense variants in SLC7A3 in 148 male patients with autism spectrum disorder (ASD), which may lead to loss of SLC7A3 function due to altered protein stability or abnormal trafficking to the plasma membrane. They suggested that SLC7A3 variants may be responsible for the etiology of ASD.
This article demonstrated that NMDA receptor activation can markedly decrease the expression of the cationic amino acid transporters CAT1 and CAT3, resultantly reducing arginine transport, which then regulates the mammalian target of rapamycin (mTOR) pathway that controls cell growth.
The authors utilized appropriate reference genes (TBP, TUBA1B, HPRT1, and ACTB) to compare the complementary results between qPCR and in situ hybridization techniques for SLC5A1 and SLC7A3 mRNAs and they revealed that SLC7A3 was expressed by the established placenta to support fetal growth.
The authors constructed consensus modules by weighted gene coexpression network analysis and discovered novel markers in undifferentiated human embryonic stem cells (hESCs) under various differentiation conditions. SLC7A3 was one top downregulated marker, which was correlated to the establishment of iPSCs.
The review summarized the structure and functions of CAT proteins (CAT for cationic amino acid transporter), including CAT-1 (SLC7A1), CAT-2A (SLC7A2A), CAT-2B (SLC7A2B), and CAT-3 (SLC7A3).
SLC7A3 Preparation Options
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