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SLC38A2 Membrane Protein Introduction

Introduction of SLC38A2

Sodium-dependent neutral amino acid transporter 2 (SNAT2, encoded by the gene SLC38A2) is a member of the system A transporter subfamily of the solute carrier family 38 (SLC38). SLC38A2 contains 504 amino acids residues with a predicted molecular mass of 56 kDa. This protein transports substrates coupled to the uptake of Na+ with a stoichiometry of 1:1. It has a very broad tissue distribution profile. The substrates include a broad range of zwitterionic, aliphatic amino acids, such as alanine, asparagine, cysteine, glutamine, glycine, histidine, methionine, proline, and serine. Structurally, hydropathy plotting indicates that SLC38A2 has 11 transmembrane helices, as is shown in figure 1.

Basic Information of SLC38A2
Protein Name Sodium-coupled neutral amino acid transporter 2
Gene Name SLC38A2
Aliases Amino acid transporter A2, Protein 40-9-1, Solute carrier family 38 member 2, System A amino acid transporter 2, System A transporter 1, System N amino acid transporter 2, ATA2, KIAA1382, SAT2, SNAT2
Organism Homo sapiens (Human)
UniProt ID Q96QD8
Transmembrane Times 11
Length (aa) 506
Sequence MKKAEMGRFSISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQALTNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSILAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLLSGVLVMTGSMALIVLDWVHNAPGGGH

Functions of SLC38A2 Membrane Protein

SLC38A2 has been reported to have many important physiological roles. The first one is the ability to be up-regulated in response to extracellular amino acid limitation. In the liver, SLC38A2 has been suggested to have a role in gluconeogenesis in the liver, since expression of SLC38A2 mRNA is strongly regulated by diabetic conditions and glucagon injections in the rat. In the brain, SLC38A2 has been suggested to be involved in glutamine transport in the glutamate/glutamine cycle in neurons with some other members of the SLC38 family. Besides, it has been shown to be important for regulation of cell volume in fibroblasts and it is reasonable to believe this regulation is important for most, if not all, cells due to the wide expression of this protein. Furthermore, SLC38A2 appears to play a role in cell growth and differentiation by signaling through the mTOR pathway. There is also evidence that SLC38A2 is up-regulated in cancer, for instance, human liver cancer and prostate cancer. SLC38A2 is required to support glutaminolysis in cancer cells.

The SLC38 family, including SLC38A2, is involved in glutamate-glutamine cycling in the liver. Fig.1 The SLC38 family, including SLC38A2, is involved in glutamate-glutamine cycling in the liver. (Schiöth, 2013)

Application of SLC38A2 Membrane Protein in Literature

  1. Nardi F., et al. Proteasomal modulation of cellular SNAT2 (SLC38A2) abundance and function by unsaturated fatty acid availability. Journal of Biological Chemistry. 2015, 290(13): 8173-84. PubMed ID: 25653282

    This study demonstrated that when cells were pretreated with linoleic acid, the adaptive increase of SNAT2 expression and function induced by amino acid deprivation and hypertonicity can be significantly suppressed by promoting its degradation via the ubiquitin-proteasome system.

  2. Li G., et al. Characterization and regulation of the amino acid transporter SNAT2 in the small intestine of piglets. PloS one. 2015, 10(6): e0128207. PubMed ID: 26107628

    This study investigated the characteristics and regulation of SNAT2 in the small intestine of piglets using sequence alignment, phylogenetic analysis, and RT-PCR.

  3. Chen C., et al. Identification of a Disulfide Bridge in Sodium-Coupled Neutral Amino Acid Transporter 2 (SNAT2) by Chemical Modification. PloS one. 2016, 11(6): e0158319. PubMed ID: 27355203

    Using chemical modification that induced mutagenesis of cysteine, this study investigated the potential of intrinsic cysteines to form disulfide bonds in SNAT2. The results showed that a disulfide bond between Cys245 and Cys279 in SNAT2 had no effect on both cell surface trafficking and transporter function.

  4. Velázquez-Villegas L.A., et al. Prolactin and the dietary protein/carbohydrate ratio regulate the expression of SNAT2 amino acid transporter in the mammary gland during lactation. Biochimica et Biophysica Acta (BBA)-Biomembranes. 2015, 1848(5): 1157-1164. PubMed ID: 25701231

    This study investigated the amount and localization of SNAT2 before delivery and during lactation in rat mammary gland (MG), as well as whether prolactin and the dietary protein/carbohydrate ratio might influence SNAT2 expression in the MG, liver and adipose tissue during lactation.

  5. Nishimura T., et al. System A amino acid transporter SNAT2 shows subtype-specific affinity for betaine and hyperosmotic inducibility in placental trophoblasts. Biochimica et Biophysica Acta (BBA)-Biomembranes. 2014, 1838(5): 1306-1312. PubMed ID: 24434061

    This study investigated the subtypes of system A SNATs that were involved in hypertonicity-induced betaine uptake mediation using HEK293 cells transiently transfected with human or rat SNAT1-4. The results showed that SNAT2 was involved in the regulation of betaine concentration in placental trophoblasts.

SLC38A2 Preparation Options

Supported by our unparalleled Magic™ membrane protein production platform, Creative Biolabs now provides custom-oriented services for reconstitution of membrane proteins into different mimetics. In different cases, different systems should be selected. Detergents are the most widely used tools for membrane protein solubilization and isolation but may disrupt the native structures and bioactivity. The recently developed techniques that use nanodiscs and polymers can better keep the membrane proteins correctly folded while maintaining the functions. Our scientists have accumulated years of experience in the whole process of membrane protein expression, solubilization, stabilization, and characterization and we are happy to share our expertise with our clients.

Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC38A2 antibody development services.


Contact us if you want to know more about our membrane protein preparation services.

Reference

  1. Schiöth H B, et al. (2013). Evolutionary origin of amino acid transporter families SLC32, SLC36 and SLC38 and physiological, pathological and therapeutic aspects. Molecular aspects of medicine. 34(2-3): 571-585.

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