SLC36A2 Membrane Protein Introduction

Introduction of SLC36A2

Proton-coupled amino acid transporter 2 (SLC36A2 or PAT2) belongs to the solute carrier family 36. It is a rheogenic H⁺ coupled transporter for small, unbranched, dipolar amino and imino acids. The substrates of PAT2 include glycine, alanine, L- and D-proline, trans-4-hydroxyproline, sarcosine, and the amino acid derivative alpha(methyl)aminoisobutyric acid (MeAIB). The transport of SLC36A2 for amino acid derivatives has a narrower substrate selectivity but higher affinity than SLC36A1. In human, SLC36A2 mRNA expression is detected in the kidney and skeletal muscle. Specifically, it is expressed in the S1 segment of the proximal tubule close to the glomerulus. The transport of PAT2 is pH-dependent but the maximal transport is not likely to be altered greatly by changes within the range of pH 7.4-9.3. The gene SLC36A2 is located on human chromosome 5q33.1. The protein comprises 483 amino acids in length and structurally have 11 transmembrane domains.

Functions of SLC36A2 Membrane Protein

SLC36A2 is expressed at the apical membrane in the renal proximal tubule and is one of the transport systems that are involved in reabsorption of amino acids and derivatives (glycine, proline, and hydroxyproline) from the renal filtrate. Mutations or dysfunction of this protein cause iminoglycinuria (characterized by excess urinary proline, hydroxyproline, and glycine) and hyperglycinuria (characterized by isolated excess urinary glycine). But studies have shown that the inheritance patterns of mutations leading to these disorders are complex. Further, the transport of drugs via this carrier will be affected, which, in turn, will influence the renal reabsorption and the pharmacokinetics of these drugs.

Application of SLC36A2 Membrane Protein in Literature

1. Zebisch K. and Brandsch M. Transport of L-proline by the proton-coupled amino acid transporter PAT2 in differentiated 3T3-L1 cells. Amino acids. 2013, 44(2): 373-381. PubMed ID: 22711289
   
   

   This study investigates the mechanism and substrate specificity of the PAT2 in 3T3-L1 cells using different substrates such as glycine, L-alanine, and L-tryptophan. The PAT2 is expressed in the 3T3-L1 adipocytes.

2. Edwards N., et al. Amino acid derivatives are substrates or non-transported inhibitors of the amino acid transporter PAT2 (slc36a2). BBA-Biomembranes. 2011, 1808(1): 260-270. PubMed ID: 20691150
   
   

   Using various proline, GABA and tryptophan derivatives, this study investigates if they function either as transported substrates or non-transported inhibitors of PAT2 following heterologous expression of rat PAT2 in Xenopus laevis oocytes.

3. Ussar S., et al. ASC-1, PAT2, and P2RX5 are cell surface markers for white, beige, and brown adipocytes. Science translational medicine. 2014, 6(247): 247ra103-247ra103. PubMed ID: 25080478
   
   

   This study identifies the membrane surface protein PAT2, together with ASC-1 and P2RX5, like new cell surface markers of adipose cell types using a combination of in silico, in vitro, and in vivo methods.

4. Rubio-Aliaga I., et al. The proton/amino acid cotransporter PAT2 is expressed in neurons with a different subcellular localization than its paralog PAT1. Journal of Biological Chemistry. 2004, 279(4): 2754-2760. PubMed ID: 14600155
   
   

   This study investigates the tissue distribution of the PAT2 protein. The results show that this protein is expressed in the spinal cord and brain, contributing to neuronal transport and sequestration of amino acids. The transport direction can be bidirectional, which is dependent on different forces like substrate concentration, pH gradient, and membrane potential.

5. Vanslambrouck J.M., et al. Renal imino acid and glycine transport system ontogeny and involvement in developmental iminoglycinuria. Biochemical Journal. 2010, 428(3): 397-407. PubMed ID: 20377526
   
   

   This study identifies the transporters that are involved in developmental iminoglycinuria and their contribution to renal reabsorption capacity. In addition, the results show that the Slc6a18, Slc6a19, Slc6a20a, and Slc36a2 have delayed expression and maturation in neonatal mice, which might be the molecular mechanism of developmental iminoglycinuria.

SLC36A2 Preparation Options

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