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Function and structure of heterodimeric amino acid transporters

Wagner, Carsten; Lang, Florian; Broer, Stefan

Description

Heterodimeric amino acid transporters are comprised of two subunits, a polytopic membrane protein (light chain) and an associated type II membrane protein (heavy chain). The heavy chain rbAT (related to bo,+ amino acid transporter) associates with the light chain bo,+ AT (bo,+ amino acid transporter) to form the amino acid transport system bo,+, whereas the homologous heavy chain 4F2hc interacts with several light chains to form system L (with LAT1 and LAT2), system y+L (with y+LAT1 and...[Show more]

dc.contributor.authorWagner, Carsten
dc.contributor.authorLang, Florian
dc.contributor.authorBroer, Stefan
dc.date.accessioned2015-12-10T23:20:31Z
dc.date.available2015-12-10T23:20:31Z
dc.identifier.issn0363-6143
dc.identifier.urihttp://hdl.handle.net/1885/66362
dc.description.abstractHeterodimeric amino acid transporters are comprised of two subunits, a polytopic membrane protein (light chain) and an associated type II membrane protein (heavy chain). The heavy chain rbAT (related to bo,+ amino acid transporter) associates with the light chain bo,+ AT (bo,+ amino acid transporter) to form the amino acid transport system bo,+, whereas the homologous heavy chain 4F2hc interacts with several light chains to form system L (with LAT1 and LAT2), system y+L (with y+LAT1 and y+LAT2), system xc- (with xAT), or system asc (with asc1). The association of light chains with the two heavy chains is not unambiguous. rbAT may interact with LAT2 and y+LAT1 and vice versa; 4F2hc may interact with bo,+ AT when overexpressed. 4F2hc is necessary for trafficking of the light chain to the plasma membrane, whereas the light chains are thought to determine the transport characteristics of the respective heterodimer. In contrast to 4F2hc, mutations in rbAT suggest that rbAT itself takes part in the transport besides serving for the trafficking of the light chain to the cell surface. Heavy and light subunits are linked together by a disulfide bridge. The disulfide bridge, however, is not necessary for the trafficking of rbAT or 4F2 heterodimers to the membrane or for the functioning of the transporter. However, there is experimental evidence that the disulfide bridge in the 4F2hc/LAT1 heterodimer plays a role in the regulation of a cation channel. These results highlight complex interactions between the different subunits of heterodimeric amino acid transporters and suggest that despite high grades of homology, the interactions between rbAT and 4F2hc and their respective partners may be different.
dc.publisherAmerican Physiological Society
dc.sourceAmerican Journal of Physiology - Cell Physiology
dc.subjectKeywords: amino acid transport; cell differentiation; cell growth; disulfide bond; human; nonhuman; priority journal; review; sequence homology; structure activity relation; Amino Acid Transport Systems; Animals; Biological Transport; Carrier Proteins; Humans; Mole Cystinuria; Disulfide bridge; Heavy and light chains; Lysinuric protein intolerance
dc.titleFunction and structure of heterodimeric amino acid transporters
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume281
dc.date.issued2001
local.identifier.absfor060110 - Receptors and Membrane Biology
local.identifier.ariespublicationMigratedxPub1270
local.type.statusPublished Version
local.contributor.affiliationWagner, Carsten, University of Zurich
local.contributor.affiliationLang, Florian, University of Tubingen
local.contributor.affiliationBroer, Stefan, College of Medicine, Biology and Environment, ANU
local.bibliographicCitation.issue4
local.bibliographicCitation.startpage1077
local.bibliographicCitation.lastpage1093
dc.date.updated2015-12-10T10:24:53Z
local.identifier.scopusID2-s2.0-0034796442
CollectionsANU Research Publications

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