Abstract
Solute carriers form one of three major superfamilies of membrane transporters in humans, and include uniporters, exchangers and symporters. Following several decades of molecular characterisation, multiple solute carriers that form obligatory heteromers with unrelated subunits are emerging as a distinctive principle of membrane transporter assembly. Here we comprehensively review experimentally established heteromeric solute carriers: SLC3-SLC7 amino acid exchangers, SLC16 monocarboxylate/H+ symporters and basigin/embigin, SLC4A1 (AE1) and glycophorin A exchanger, SLC51 heteromer Ost α-Ost β uniporter, and SLC6 heteromeric symporters. The review covers the history of the heteromer discovery, transporter physiology, structure, disease associations and pharmacology – all with a focus on the heteromeric assembly. The cellular locations, requirements for complex formation, and the functional role of dimerization are extensively detailed, including analysis of the first complete heteromer structures, the SLC7-SLC3 family transporters LAT1-4F2hc, b0,+AT-rBAT and the SLC6 family heteromer B0AT1-ACE2. We present a systematic analysis of the structural and functional aspects of heteromeric solute carriers and conclude with common principles of their functional roles and structural architecture.
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Notes
- 1.
This distinction is important as numerous publications use the residue numbering of either isoform 1 or 2 without distinguishing between them. Isoform 2 (UniPROT P08195-2) differs from isoform 1 (UniPROT P08195-1) by having cytosolic, N-terminal residues 1–101 missing.
- 2.
Note that the numbering used in both structure publications are derived from UniPROT designated isoform 1 of human 4F2hc (P08195-1). However, there are also minor mistakes in each manuscript: Nureki and colleagues have mislabelled 4F2hc R434 as R511 when describing the Cβ2/Cβ3/Cβ8-linker-EL2 interaction network, while Yan and colleagues have miss-assigned all 4F2hc residues by an increase of 1 in their manuscript.
- 3.
Note: the residue numbering quoted for glycophorin A in publications cited here was based on the protein sequence less residues 1–19, the signal peptide (i.e. 131 residues). The correct numbering of the full 150 residue glycophorin A amino acid sequence is given in brackets.
- 4.
Type IV have the same orientation as type II except the C-terminal TM domain is a signal anchor.
- 5.
As collectrin and ACE2 are located on the X chromosome, the male collectrin/ACE2 null mouse is a (−/y) genotype while the female is a collectrin/ACE2 mouse (−/−).
Abbreviations
- AA:
-
Amino Acids
- APC:
-
Amino Acid-Polyamine-Organocation Transporter Family
- APN:
-
Aminopeptidase N
- ACE2:
-
Angiotensin Converting Enzyme 2
- AE1:
-
Anion Exchanger 1
- mAbs:
-
monoclonal Antibodies
- ADHD:
-
Attention Deficit Hyperactivity Disorder
- ASD:
-
Autism Spectrum Disorder
- BCH:
-
2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid
- B0AT1/3:
-
Broad Neutral Amino acid Transporter 1/3
- CA:
-
Carbonic Anhydrase
- CD:
-
Cluster of Differentiation
- CHS:
-
Cholesterol hemisuccinate
- DHEAS:
-
Dehydroepiandrosterone
- DAT:
-
Dopamine Transporter
- EC:
-
Extracellular
- ER:
-
Endoplasmic Reticulum
- ERAD:
-
Endoplasmic Reticulum Associated Degradation
- FGF:
-
Fibroblast Growth Factor
- FXR:
-
Farnesoid X receptor
- GAT:
-
GABA Transporter
- GSH:
-
Glutathione
- GLYT1/2:
-
Glycine Transporter 1/2
- GPA/B/C:
-
Glycophorin A/B/C
- HS:
-
Hereditary Spherocytosis
- HMM:
-
Hidden Markov Model
- ISF:
-
Insulin Sensitivity Factor
- KO:
-
Knock-out
- L-DOPA:
-
L-3,4-dihydroxyphenylalanine
- LPI:
-
Lysinuria Protein Intolerance
- MeAIB:
-
Methylaminoisobutyric acid
- MCT:
-
Monocarboxylate Transporter
- NFPS:
-
N-[3-(4′-fluorophenyl)-3-(4′-phenylphenoxy)-propyl]sarcosine
- NET:
-
Noradrenaline Epinephrine Transporter
- NSS:
-
Neurotransmitter Sodium Symporter
- OMIM:
-
Online Mendelian Inheritance in Man
- pCMBS:
-
p-chloromercuribenzene sulphonate
- PPI:
-
Protein-Protein Interaction
- RBC:
-
Red Blood Cell
- dRTA:
-
distal Renal Tubular Acidosis
- RPE:
-
Retinal Pigment Epithelium
- RdCVF:
-
Rod-derived Cone Viability Factor
- SERT:
-
Serotonin Transporter
- SAO:
-
Southeast Asian Ovalcytosis
- SAR:
-
Stramenopiles [heterokonts] Alveolates and Rhizaria supergroup
- TCDB:
-
Transporter Classification Database
- TM:
-
Transmembrane
- T3:
-
Triiodothyronine
- T4:
-
Thyroxine
- TEM:
-
Transmission Electron Microscopy
- VDW:
-
Van der Waals
- YFP:
-
Yellow Fluorescent Protein
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Acknowledgements
We thank all the members of the Bröer Laboratory of Membrane Transporters and Nutrition at the Australian National University for feedback and comments. We also acknowledge and thank Professor Manuel Palacin and Dr. Ekaitz Errasti in the Amino Acid Transporters and Disease Laboratory at the Institute for Research in Biomedicine (IRB) for providing their models of LAT2-4F2hc. We have attempted to write the first comprehensive review on the subject of heteromeric solute carriers. We apologise for the omission of any relevant references, which is unintentional, and encourage authors to contact us in order that we can rectify any omissions for future updated additions of the review.
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Fairweather, S.J., Shah, N., Brӧer, S. (2020). Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology. In: Atassi, M.Z. (eds) Protein Reviews . Advances in Experimental Medicine and Biology(), vol 21. Springer, Cham. https://doi.org/10.1007/5584_2020_584
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