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Membrane Topology of Rat Sodium-Coupled Neutral Amino Acid Transporter 2 (SNAT2)

Membrane Topology of Rat Sodium-Coupled Neutral Amino Acid Transporter 2 (SNAT2)

Yudan Ge, Yanting Gu, Jiahong Wang, Zhou Zhang

Biochim Biophys Acta Biomembr. 2018 Jul;1860(7):1460-1469.

PMID: 29678469

Abstract:

Sodium-coupled neutral amino acid transporter 2 (SNAT2) is a subtype of the amino acid transport system A that is widely expressed in mammalian tissues. It plays critical roles in glutamic acid-glutamine circulation, liver gluconeogenesis and other biological pathway. However, the topology of the SNAT2 amino acid transporter is unknown. Here we identified the topological structure of SNAT2 using bioinformatics analysis, Methoxy-polyethylene glycol maleimide (mPEG-Mal) chemical modification, protease cleavage assays, immunofluorescence and examination of glycosylation. Our results show that SNAT2 contains 11 transmembrane domains (TMDs) with an intracellular N terminus and an extracellular C terminus. Three N-glycosylation sites were verified at the largest extracellular loop. This model is consistent with the previous model of SNAT2 with the exception of a difference in number of glycosylation sites. This is the first time to confirm the SNAT2 membrane topology using experimental methods. Our study on SNAT2 topology provides valuable structural information of one of the solute carrier family 38 (SLC38) members.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP99126644	Methoxypolyethylene glycol maleimide		99126-64-4	Price

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