Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family

<p>Abstract</p> <p>Background</p> <p>In general, sugar porters function by proton-coupled symport or facilitative transport modes. Symporters, coupled to electrochemical energy, transport nutrients against a substrate gradient. Facilitative carriers transport sugars alo...

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Main Authors: Patron Nicola, Wilson-O'Brien Amy L, Rogers Suzanne
Format: Article
Language:English
Published: BMC 2010-05-01
Series:BMC Evolutionary Biology
Online Access:http://www.biomedcentral.com/1471-2148/10/152
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spelling doaj-95137016d11d4a308b08f24555a8f92c2021-09-02T03:54:27ZengBMCBMC Evolutionary Biology1471-21482010-05-0110115210.1186/1471-2148-10-152Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) familyPatron NicolaWilson-O'Brien Amy LRogers Suzanne<p>Abstract</p> <p>Background</p> <p>In general, sugar porters function by proton-coupled symport or facilitative transport modes. Symporters, coupled to electrochemical energy, transport nutrients against a substrate gradient. Facilitative carriers transport sugars along a concentration gradient, thus transport is dependent upon extracellular nutrient levels. Across bacteria, fungi, unicellular non-vertebrates and plants, proton-coupled hexose symport is a crucial process supplying energy under conditions of nutrient flux. In mammals it has been assumed that evolution of whole body regulatory mechanisms would eliminate this need. To determine whether any isoforms bearing this function might be conserved in mammals, we investigated the relationship between the transporters of animals and the proton-coupled hexose symporters found in other species.</p> <p>Results</p> <p>We took a comparative genomic approach and have performed the first comprehensive and statistically supported phylogenetic analysis of all mammalian glucose transporter (GLUT) isoforms. Our data reveals the mammalian GLUT proteins segregate into five distinct classes. This evolutionary ancestry gives insight to structure, function and transport mechanisms within the groups. Combined with biological assays, we present novel evidence that, in response to changing nutrient availability and environmental pH, proton-coupled, active glucose symport function is maintained in mammalian cells.</p> <p>Conclusions</p> <p>The analyses show the ancestry, evolutionary conservation and biological importance of the GLUT classes. These findings significantly extend our understanding of the evolution of mammalian glucose transport systems. They also reveal that mammals may have conserved an adaptive response to nutrient demand that would have important physiological implications to cell survival and growth.</p> http://www.biomedcentral.com/1471-2148/10/152
collection DOAJ
language English
format Article
sources DOAJ
author Patron Nicola
Wilson-O'Brien Amy L
Rogers Suzanne
spellingShingle Patron Nicola
Wilson-O'Brien Amy L
Rogers Suzanne
Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family
BMC Evolutionary Biology
author_facet Patron Nicola
Wilson-O'Brien Amy L
Rogers Suzanne
author_sort Patron Nicola
title Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family
title_short Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family
title_full Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family
title_fullStr Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family
title_full_unstemmed Evolutionary ancestry and novel functions of the mammalian glucose transporter (GLUT) family
title_sort evolutionary ancestry and novel functions of the mammalian glucose transporter (glut) family
publisher BMC
series BMC Evolutionary Biology
issn 1471-2148
publishDate 2010-05-01
description <p>Abstract</p> <p>Background</p> <p>In general, sugar porters function by proton-coupled symport or facilitative transport modes. Symporters, coupled to electrochemical energy, transport nutrients against a substrate gradient. Facilitative carriers transport sugars along a concentration gradient, thus transport is dependent upon extracellular nutrient levels. Across bacteria, fungi, unicellular non-vertebrates and plants, proton-coupled hexose symport is a crucial process supplying energy under conditions of nutrient flux. In mammals it has been assumed that evolution of whole body regulatory mechanisms would eliminate this need. To determine whether any isoforms bearing this function might be conserved in mammals, we investigated the relationship between the transporters of animals and the proton-coupled hexose symporters found in other species.</p> <p>Results</p> <p>We took a comparative genomic approach and have performed the first comprehensive and statistically supported phylogenetic analysis of all mammalian glucose transporter (GLUT) isoforms. Our data reveals the mammalian GLUT proteins segregate into five distinct classes. This evolutionary ancestry gives insight to structure, function and transport mechanisms within the groups. Combined with biological assays, we present novel evidence that, in response to changing nutrient availability and environmental pH, proton-coupled, active glucose symport function is maintained in mammalian cells.</p> <p>Conclusions</p> <p>The analyses show the ancestry, evolutionary conservation and biological importance of the GLUT classes. These findings significantly extend our understanding of the evolution of mammalian glucose transport systems. They also reveal that mammals may have conserved an adaptive response to nutrient demand that would have important physiological implications to cell survival and growth.</p>
url http://www.biomedcentral.com/1471-2148/10/152
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