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

BMC Evolutionary Biology

Research Article

Nicola Patron¹  Amy L Wilson-O'Brien²  Suzanne Rogers³ 

[1] Department of Botany, The University of Melbourne, 3052, Parkville, Victoria, Australia;Department of Primary Industries, Victorian Agribiosciences Centre, 3983, Bundoora, Victoria, Australia;Department of Medicine-St. Vincent's, The University of Melbourne, 3065, Fitzroy, Victoria, Australia;Department of Genetics, The University of Melbourne, 3052, Parkville, Victoria, Australia;Department of Medicine-St. Vincent's, The University of Melbourne, 3065, Fitzroy, Victoria, Australia;Protein Chemistry and Metabolism Unit, St. Vincent's Institute of Medical Research, 3065, Fitzroy, Victoria, Australia;

关键词: Glucose Transport;    Madin Darby Canine Kidney;    Madin Darby Canine Kidney Cell;    Glucose Gradient;    Evolutionary Ancestry;   

DOI  :  10.1186/1471-2148-10-152

 received in 2009-10-15, accepted in 2010-05-21,  发布年份 2010

来源: Springer

【 摘 要 】

BackgroundIn 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.ResultsWe 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.ConclusionsThe 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.

【 授权许可】

Unknown   
© Wilson-O'Brien et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.