The major facilitator superfamily member Slc37a2 is a novel macrophage- specific gene selectively expressed in obese white adipose tissue

Kim, Ji Young; Tillison, Kristin; Zhou, Shengli; Wu, Yuzhang; Smas, Cynthia M.

doi:10.1152/ajpendo.00404.2006

Cited by 22 publications

(41 citation statements)

References 59 publications

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“…The solute carrier 37 (SLC37) family consists of 4 proteins, SLC37A1 [13]–[15], SLC37A2 [15]–[17], SLC37A3 [15] and G6PT/SLC37A4 [5], [6], [15]. With the exception of G6PT, which was shown to function as a P i -linked G6P antiporter [3], none of the other SLC37 proteins has been functionally characterized.…”

Section: Introductionmentioning

confidence: 99%

SLC37A1 and SLC37A2 Are Phosphate-Linked, Glucose-6-Phosphate Antiporters

et al. 2011

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Blood glucose homeostasis between meals depends upon production of glucose within the endoplasmic reticulum (ER) of the liver and kidney by hydrolysis of glucose-6-phosphate (G6P) into glucose and phosphate (Pi). This reaction depends on coupling the G6P transporter (G6PT) with glucose-6-phosphatase-α (G6Pase-α). Only one G6PT, also known as SLC37A4, has been characterized, and it acts as a Pi-linked G6P antiporter. The other three SLC37 family members, predicted to be sugar-phosphate:Pi exchangers, have not been characterized functionally. Using reconstituted proteoliposomes, we examine the antiporter activity of the other SLC37 members along with their ability to couple with G6Pase-α. G6PT- and mock-proteoliposomes are used as positive and negative controls, respectively. We show that SLC37A1 and SLC37A2 are ER-associated, Pi-linked antiporters, that can transport G6P. Unlike G6PT, neither is sensitive to chlorogenic acid, a competitive inhibitor of physiological ER G6P transport, and neither couples to G6Pase-α. We conclude that three of the four SLC37 family members are functional sugar-phosphate antiporters. However, only G6PT/SLC37A4 matches the characteristics of the physiological ER G6P transporter, suggesting the other SLC37 proteins have roles independent of blood glucose homeostasis.

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Section: Introductionmentioning

confidence: 99%

SLC37A1 and SLC37A2 Are Phosphate-Linked, Glucose-6-Phosphate Antiporters

et al. 2011

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“…SLC37A1 or SPX1 (Bartoloni & Antonarakis, 2004; Bartoloni et al, 2000; Chou et al, 2013; Iacopetta et al, 2010; Pan et al, 2011), SLC37A2 or SPX2 (Bartoloni & Antonarakis, 2004; Chou et al, 2013; Kim, Tillison, Zhou, Wu, & Smas, 2007; Pan et al, 2011; Takahashi et al, 2000), and SLC37A3 or SPX3 (Bartoloni & Antonarakis, 2004; Chou et al, 2013; Pan et al, 2011) are the less characterized members of the SLC37 family. Human SLC37A1, SLC37A2, and SLC37A3 are similar to G6PT in being ER-associated transmembrane proteins (Pan et al, 2011).…”

Section: Slc37a1 Slc37a2 and Slc37a3mentioning

confidence: 99%

“…The murine Slc37a2 was first identified as a cAMP-inducible gene in RAW264 macrophages (Takahashi et al, 2000). The 510 amino acid murine Slc37a2 protein contains three potential N-linked glycosylation sites and migrates as a heterogeneous species of 55–75 kDa (Kim et al, 2007). In this respect, it differs from the nonglycosylated SLC37A1, SLC37A3, and SLC37A4.…”

Section: Slc37a1 Slc37a2 and Slc37a3mentioning

confidence: 99%

“…In this respect, it differs from the nonglycosylated SLC37A1, SLC37A3, and SLC37A4. The Slc37a2 transcript in mice is primarily expressed in the spleen, thymus, and macrophages (Kim et al, 2007). Compared to Slc37a4 , the Slc37a2 transcript is highly expressed in neutrophils and macrophages.…”

Section: Slc37a1 Slc37a2 and Slc37a3mentioning

confidence: 99%

“…Compared to Slc37a4 , the Slc37a2 transcript is highly expressed in neutrophils and macrophages. Human SLC37A2 is post-translationally modified by N-linked glycosylation, and the human SLC37A2 transcript increases markedly during differentiation of THP-1 human monocytes to macrophages (Kim et al, 2007). The tissue-specific expression of SLC37A2 in macrophages and neutrophils may point to a biological transport role in these cells.…”

Section: Slc37a1 Slc37a2 and Slc37a3mentioning

confidence: 99%

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The SLC37 Family of Sugar-Phosphate/Phosphate Exchangers

Chou

Mansfield

2014

Current Topics in Membranes

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The SLC37 family members are endoplasmic reticulum (ER)-associated sugar-phosphate/phosphate (Pi) exchangers. Three of the four members, SLC37A1, SLC37A2, and SLC37A4, function as Pi-linked glucose-6-phosphate (G6P) antiporters catalyzing G6P:Pi and Pi:Pi exchanges. The activity of SLC37A3 is unknown. SLC37A4, better known as the G6P transporter (G6PT), has been extensively characterized, functionally and structurally, and is the best characterized family member. G6PT contains 10 transmembrane helices with both N and C termini facing the cytoplasm. The primary in vivo function of the G6PT protein is to translocate G6P from the cytoplasm into the ER lumen where it couples with either the liver/kidney/intestine-restricted glucose-6-phosphatase-α (G6Pase-α or G6PC) or the ubiquitously expressed G6Pase-β (or G6PC3) to hydrolyze G6P to glucose and Pi. The G6PT/G6Pase-α complex maintains interprandial glucose homeostasis, and the G6PT/G6Pase-β complex maintains neutro-phil energy homeostasis and functionality. G6PT is highly selective for G6P and is competitively inhibited by cholorogenic acid and its derivatives. Neither SLC37A1 nor SLC37A2 can couple functionally with G6Pase-α or G6Pase-β, and the antiporter activities of SLC37A1 or SLC37A2 are not inhibited by cholorogenic acid. Deficiencies in G6PT cause glycogen storage disease type Ib (GSD-Ib), a metabolic and immune disorder. To date, 91 separate SLC37A4 mutations, including 39 missense mutations, have been identified in GSD-Ib patients. Characterization of missense mutations has yielded valuable information on functionally important residues in the G6PT protein. The biological roles of the other SLC37 proteins remain to be determined and deficiencies have not yet been correlated to diseases.

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The sugar phosphate/phosphate exchanger family SLC37

Olcese

Bartoloni²

2013

WIREs Membr Transp Signal

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The solute-carrier (SLC) superfamily is divided into 55 different families of genes coding for integral membrane proteins, which transport not only all kinds of endogenous solute substrates, but also exogenous drugs and chemicals. The SLC37 transporters are members of the organophosphate:Pi antiporter family (OPA) and therefore they belong to the major facilitator superfamily (MFS). The SLC37 family members diverged early in evolution. SLC37A1 and SLC37A2 transporters are closely related and they have 57% of identical amino acids, while they have an average of 31% identical amino acids with SLC37A3. SLC37A4 is however quite different from them, sharing an average of 15% identity with the other three members. The SLC37A4 gene (also known as glucose-6-phosphate transporter, G6PT) is mutated in the glycogen storage disease non-1A type, therefore it is well studied both at the DNA and protein levels. Major function of SLC37A4 is to preserve interprandial glucose homeostasis. Data on SLC37A1 and SLC37A2 genes expression are available both in humans and in mice, but there is still little information on their protein function. Even if they are homologous to glycerol-3-phosphate transporters, they were described to transport glucose-6-phosphate; therefore, they might be multisolute carriers. SLC37A3 is still poorly investigated and the only described feature is that it seems not to transport glucose-6-phosphate.

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The major facilitator superfamily member Slc37a2 is a novel macrophage- specific gene selectively expressed in obese white adipose tissue

Cited by 22 publications

References 59 publications

SLC37A1 and SLC37A2 Are Phosphate-Linked, Glucose-6-Phosphate Antiporters

SLC37A1 and SLC37A2 Are Phosphate-Linked, Glucose-6-Phosphate Antiporters

The SLC37 Family of Sugar-Phosphate/Phosphate Exchangers

The sugar phosphate/phosphate exchanger family SLC37

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