Structure of, and functional insight into the GLUT family of membrane transporters

Long, Wentong; Cheeseman, Chris I.

doi:10.2147/chc.s60484

Cited by 28 publications

(17 citation statements)

References 167 publications

(256 reference statements)

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“…This proposed transport mechanism assumes that GLUT transporters have a substrate cavity and binding site, as well as one intracellular and one extracellular configuration opening. The crystal structure of GLUT1 is consistent with and supports this alternating access mechanism (Long and Cheeseman 2015).…”

Section: Structure and Function Of Glut Class Memberssupporting

confidence: 73%

Gab1

Vaillancourt¹,

Spilker²,

Park³

2018

Encyclopedia of Signaling Molecules

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G alpha o 1893G regulators of the Gao protein may provide a cellspecific mechanism for Gao-regulated signaling pathways. PTX catalyzes the ADP-ribosylation of the a subunits of the Go, Gi, and Gt proteins at the C-terminal cysteine residue (À4 position). This prevents the G protein from interacting with GPCRs on the cell membrane, thus interfering with intracellular signaling. 1896 G alpha o G alpha o 1897 G cyclase, guanylate cyclase, Rap1 GTPaseactivating protein (Rap1GAP), axin, and pins. Compartmentalization of these signaling molecules in membrane rafts may ensure specificity and fidelity in Gao signaling. Go is the most abundant G protein in the central nervous system, where it comprises about 1% of membrane proteins in the mammalian brain. Go regulates neuronal development, memory, visual reception, olfactory reception, and taste reception. It is also localized in heart tissue and implicated in heart contractility. Its expression is regulated during the development of the brain and heart. Somatic mutations in the GNAO1 gene induce human cancers by rendering Gao constitutively activated. Heterozygous mutations in the GNAO1 gene cause epileptic encephalopathy by destabilizing Gao. Gao-deficient mice have several neurological deficits, including tremors, seizures, hyperalgesia, motor control impairment, and olfactory impairment. Muscarinic regulation of heart rate and heart rate variability is also impaired in Gao-deficient mice. Drosophila melanogaster mutants with loss of function of Gao show impaired morphogenesis of the heart and epithelial polarity of cardiac cells and abnormal sleep. Gao-deficient C. elegans has phenotypes including neuronal migration defects, hyperactive locomotion, and egg laying.

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Section: Structure and Function Of Glut Class Memberssupporting

confidence: 73%

Gab1

Vaillancourt¹,

Spilker²,

Park³

2018

Encyclopedia of Signaling Molecules

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“…Glucose supply of the retina is mainly mediated by glucose transporters (Hsu and Molday, 1991;Gospe et al, 2010), which are expressed in vasculature, RPE cells, PhRs and in MGCs (Watanabe et al, 1996;Wong-Riley, 2010;Veys et al, 2020; Figure 4). GLUTs are facilitative transporters and as such glucose follows a concentration gradient (Cheeseman and Long, 2015;Holman, 2020). Glucose from the blood supply leaves the choroidal endothelium and diffuses through RPE cells into the photoreceptor layer where photoreceptors take it up and readily metabolize it.…”

Section: Retinal Energy Metabolismmentioning

confidence: 99%

A Metabolic Landscape for Maintaining Retina Integrity and Function

Viegas

Neuhauss

2021

Front. Mol. Neurosci.

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Neurons have high metabolic demands that are almost exclusively met by glucose supplied from the bloodstream. Glucose is utilized in complex metabolic interactions between neurons and glia cells, described by the astrocyte-neuron lactate shuttle (ANLS) hypothesis. The neural retina faces similar energy demands to the rest of the brain, with additional high anabolic needs to support continuous renewal of photoreceptor outer segments. This demand is met by a fascinating variation of the ANLS in which photoreceptors are the central part of a metabolic landscape, using glucose and supplying surrounding cells with metabolic intermediates. In this review we summarize recent evidence on how neurons, in particular photoreceptors, meet their energy and biosynthetic requirements by comprising a metabolic landscape of interdependent cells.

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“…In addition to glucose, GLUTs supply cells with galactose, fructose, and other sugars. The transport kinetics and affinity for sugars differ between GLUTs, with the majority taking up more than one substrate and selected few showing substrate specificities [ 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Targeting of GLUT5 for Transporter-Mediated Drug-Delivery Is Contingent upon Substrate Hydrophilicity

Nahrjou

Ghosh

Tanasova

2021

IJMS

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Specific link between high fructose uptake and cancer development and progression highlighted fructose transporters as potential means to achieve GLUT-mediated discrimination between normal and cancer cells. The gained expression of fructose-specific transporter GLUT5 in various cancers offers a possibility for developing cancer-specific imaging and bioactive agents. Herein, we explore the feasibility of delivering a bioactive agent through cancer-relevant fructose-specific transporter GLUT5. We employed specific targeting of GLUT5 by 2,5-anhydro-D-mannitol and investigated several drug conjugates for their ability to induce cancer-specific cytotoxicity. The proof-of-concept analysis was carried out for conjugates of chlorambucil (CLB) in GLUT5-positive breast cancer cells and normal breast cells. The cytotoxicity of conjugates was assessed over 24 h and 48 h, and significant dependence between cancer-selectivity and conjugate size was observed. The differences were found to relate to the loss of GLUT5-mediated uptake upon increased conjugate size and hydrophobicity. The findings provide information on the substrate tolerance of GLUT5 and highlight the importance of maintaining appropriate hydrophilicity for GLUT-mediated delivery.

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Structure of, and functional insight into the GLUT family of membrane transporters

Cited by 28 publications

References 167 publications

Gab1

Gab1

A Metabolic Landscape for Maintaining Retina Integrity and Function

Targeting of GLUT5 for Transporter-Mediated Drug-Delivery Is Contingent upon Substrate Hydrophilicity

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