The SLC45 gene family of putative sugar transporters

Vitavska, Olga; Wieczorek, Helmut

doi:10.1016/j.mam.2012.05.014

Cited by 43 publications

(39 citation statements)

References 32 publications

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“…A recent special issue of Molecular Aspects of Medicine was committed to providing a comprehensive review of the current understanding of SLC transporters from physiological, disease, and pharmaceutical perspectives (37). The following MFS families were covered in this issue: the SLC2 GLUT sugar porters (74); the SLC15 proton-coupled oligopeptide transporters (96); the SLC16 monocarboxylate transporters (34); the SLC17 organic anion transporters (87); the SLC18 vesicular neurotransmitter transporters (62); the SLC19 and SLC46 folate transporters (120); the SLC21/SLCO organic anion transporters (33); the SLC22 transporters of organic cations, anions, and zwitterions (58); the SLC29 facilitative nucleoside transporters (118); the SLC33 acetyl-CoA transporters (41); the SLC37 phosphate-linked sugar phosphate antiporters (9); the SLC43 facilitator system L-amino acid transporters (6); and the SLC45 putative sugar transporters (103). The relevance of the MFS transporters to cancer, exemplified by GLUT1, GLUT3, GLUT4, MCT1, MCT4, OCT1, OCT2, and OAT10, was also examined (18).…”

Section: Physiology Disease and Pharmaceutical Perspectivesmentioning

confidence: 99%

Structural Biology of the Major Facilitator Superfamily Transporters

Yan

2015

Annu. Rev. Biophys.

370

362

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The ancient and ubiquitous major facilitator superfamily (MFS) represents the largest secondary transporter family and plays a crucial role in a multitude of physiological processes. MFS proteins transport a broad spectrum of ions and solutes across membranes via facilitated diffusion, symport, or antiport. In recent years, remarkable advances in understanding the structural biology of the MFS transporters have been made. This article reviews the history, classification, and general features of the MFS proteins; summarizes recent structural progress with a focus on the sugar porter family transporters exemplified by GLUT1; and discusses the molecular mechanisms of substrate binding, alternating access, and cotransport coupling.

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Section: Physiology Disease and Pharmaceutical Perspectivesmentioning

confidence: 99%

Structural Biology of the Major Facilitator Superfamily Transporters

Yan

2015

Annu. Rev. Biophys.

370

362

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“…3 www.fhc.viamedica.pl during the synthesis of melanin [2,3]. SLC45A2 is a member of the putative transporter family 45A, which includes four members: SLC45A1, SLC45A2 (MATP), SLC45A3 and SLC45-A4 [4]. SLC45A2 encodes a protein with homology to plant sucrose-H+ symporters, but the transport function of SLC45A2 is not known.…”

Section: Slc45a2 Was Originally Identified As An Antigen Recognized Bmentioning

confidence: 99%

Distribution and expression of SLC45A2 in the skin of sheep with different coat colors

Wang

et al. 2016

Folia Histochem Cytobiol.

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Introduction. To investigate whether the membrane-associated transporter protein SLC45A2 is differentially expressed in the skin of sheep with different coat colors and to determine its correlation with coat color establishment in sheep. Material and methods. The expression of SLC45A2 in sheep skin samples with different coat colors was qualitatively and quantitatively analyzed by PCR amplification, RT-PCR, immunohistochemical staining and Western blotting. Results. A 193-bp SLC45A2 CDS sequence was successfully amplified from sheep skin samples with diverse coat colors. RT-PCR analysis revealed that SLC45A2 mRNA was expressed in all sheep skin samples tested, with relative expression levels of 512.74 ± 121.51 in black skin, 143.38 ± 119.31 and 1.36 ± 0.09 in black dots and white dots of piebald skin, respectively, and 1.02 ± 0.23 in white skin (p < 0.01**). Positive SLC45A2 protein bands were also detected in all skin samples by Western blot analysis, with relative expression levels of 0.85 ± ± 0.17** in black skin, 0.60 ± 0.05** and 0.34 ± 0.07 in black dots and white dots of piebald skin, respectively, and 0.20 ± 0.05 in white skin (p < 0.01**). Immunohistochemical assays revealed that SLC45A2 was expressed in the hair follicle matrix, the inner and outer root sheath, and the dermal papilla in the skin tissues with different coat colors. These patterns were quantified by optical density (OD) analysis, which yielded relative expression levels of 0.23 ± 0.11 in black skin, 0.19 ± 0.09 and 0.10 ± 0.03 in black dots and white dots of piebald skin, respectively, and 0.08 ± 0.01 in white skin (p < 0.05*). Conclusion. SLC45A2 is detectably expressed in sheep skin of all coat colors, though at significantly different levels. SLC45A2 may participate in the establishment of coat color by regulating the synthesis and trafficking of melanin.

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“…The H + /sucrose symporter was termed by FlyBase as Slc45-1 and shows a significant similarity to members of the human SLC45 family (Vitavska and Wieczorek, 2013). The evolutionary history of SCRT reveals that it, like SLC45, has a highly conserved sucrose transporter signature (R-X-G-R-R).…”

Section: A) Bmentioning

confidence: 99%

“…Black circles are sites of serines or threonines which may be targets for phosphorylation by the protein kinases. Gray circles with asterisks: R-W-G-R-R (in circle), correspond to the signature sequence for sucrose transporters (Vitavska and Wieczorek, 2013).…”

Section: Figurementioning

confidence: 99%

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Functional characterization of a putative disaccharide membrane transporter in crustacean intestine

2014

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Mechanisms of transepithelial absorption of dietary sucrose in the American lobster, Homarus americanus, were investigated to determine if disaccharide sugars can be transported across an animal gut intact. Intestines were mounted in a perfusion chamber to measure mucosal to serosal (MS) 14C‐sucrose transport. MS sucrose transport was a hyperbolic function of luminal sugar concentration, suggesting the presence of carrier‐mediated transport. Sodium‐dependent glucose transport inhibitor, phloridzin, partially decreased MS 14C‐sucrose transport, suggesting hydrolysis of 14C‐sucrose to glucose during transport. Phloretin, an inhibitor of Na+‐independent basolateral glucose transport, partially decreased MS 14C‐sucrose transport, suggesting that some 14C‐sucrose radioactivity may be transported to the blood as 14C‐glucose. Decreased MS 14C‐sucrose transport also occurred in the presence of the disaccharide trehalose. Thin‐layer chromatography (TLC) was used to identify the chemical nature of radioactively‐labeled sugars in the bath following transport and revealed that 14C‐sucrose was transported across the intestine largely as an intact molecule. Results suggest that disaccharide sugars may be transported intact across crustacean intestine and provide support for the occurrence of a disaccharide membrane transporter that has not previously been functionally characterized. Grant Funding Source: This project was supported by Agriculture and Food Research Initiative Competitive Grant no. 2010‐65

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The SLC45 gene family of putative sugar transporters

Cited by 43 publications

References 32 publications

Structural Biology of the Major Facilitator Superfamily Transporters

Structural Biology of the Major Facilitator Superfamily Transporters

Distribution and expression of SLC45A2 in the skin of sheep with different coat colors

Functional characterization of a putative disaccharide membrane transporter in crustacean intestine

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