Conservation of amino acid transporters in fungi, plants and animals

doi:10.1016/S0968-0004(01)02054-0

Trends in Biochemical Sciences

Volume 27, Issue 3, 1 March 2002, Pages 139-147

https://doi.org/10.1016/S0968-0004(01)02054-0 Get rights and content

Abstract

When comparing the transporters of three completely sequenced eukaryotic genomes – Saccharomyces cerevisiae, Arabidopsis thaliana and Homo sapiens – transporter types can be distinguished according to phylogeny, substrate spectrum, transport mechanism and cell specificity. The known amino acid transporters belong to five different superfamilies. Two preferentially Na⁺-coupled transporter superfamilies are not represented in the yeast and Arabidopsis genomes, whereas the other three groups, which often function as H⁺-coupled systems, have members in all investigated genomes. Additional superfamilies exist for organellar transport, including mitochondrial and plastidic carriers. When used in combination with phylogenetic analyses, functional comparison might aid our prediction of physiological functions for related but uncharacterized open reading frames.

Section snippets

Amino acid-polyamine-choline (APC) transporter superfamily

Among eukaryotes, amino acid transport is best understood in yeast [5]. As unicellular organisms, yeasts use a variety of transporters for nutritional uptake of amino acids and for intracellular compartmentalization. Uptake across the plasma membrane is mediated by 24 different amino acid transporters belonging to the APC superfamily (SLC7, pfam00324). All 24 members contain 12 putative membrane-spanning domains and have been functionally characterized; for example, CAN1 functions as a H⁺–Arg

Mitochondrial transporter family (MCF)

Mitochondria play an important role in amino acid metabolism and, therefore, need multiple transport systems in their membranes. Porins in the outer membrane allow passage of a wide spectrum of compounds, including amino acids. Inner membrane carriers comprising six-membrane-spanning domains belong to the mitochondrial carrier family (MCF; SLC25). In yeast, arginine and ornithine carriers (arg11p and bac1p) were identified 42, 43. MCF members potentially involved in amino acid transport are

Perspectives

Previously, a multitude of genes encoding amino acid transporters was identified by functional expression cloning. Together with the availability of the complete genome sequences of fungi, plant and humans, it is possible to provide an almost complete insight into the inventory of transporters of all three kingdoms. In combination with phylogenetic analyses of amino acid transporter superfamilies, full genome comparison provides evidence for the existence of a multitude of transporters

Acknowledgements

We are grateful to R. Panford for critical reading of the manuscript. This work was supported by grants to W.B.F. from Deutsche Forschungsgemeinschaft (Gottfried-Wilhelm Leibniz, Aminosäuretransport) and BMBF.

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Trends in Biochemical Sciences

ReviewConservation of amino acid transporters in fungi, plants and animals

Abstract

Section snippets

Amino acid-polyamine-choline (APC) transporter superfamily

Mitochondrial transporter family (MCF)

Perspectives

Acknowledgements

FEBS Lett.

Trends Plant Sci.

FEBS Lett.

J. Biol. Chem.

Curr. Opin. Cell Biol.

Curr. Opin. Genet. Dev.

Biochim. Biophys. Acta

J. Biol. Chem.

J. Biol. Chem.

FEBS Lett.

Neuron

Cell

J. Biol. Chem.

J. Biol. Chem.

An overview of membrane transport proteins in Saccharomyces cerevisiae

Yeast

Molecular biology of mammalian plasma membrane amino acid transporters

Physiol. Rev.

Unidirectional arginine transport in reconstituted plasma-membrane vesicles from yeast overexpressing CAN1

Eur. J. Biochem.

Substrate specificity and gene expression of the amino-acid permeases in Saccharomyces cerevisiae

Curr. Genet.

Seed and vascular expression of a high affinity transporter for cationic amino acids in Arabidopsis

Proc. Natl. Acad. Sci. U. S. A.

Intestinal transport of peptides and amino acids

Structure, expression, and functional analysis of a Na+-dependent glutamate aspartate transporter from rat brain

Proc. Natl. Acad. Sci. U. S. A.

Cloning and expression of a rat brain l-glutamate transporter

Nature

Review
Conservation of amino acid transporters in fungi, plants and animals

Structure, expression, and functional analysis of a Na⁺-dependent glutamate aspartate transporter from rat brain