Identification and Functional Characterization of a Novel Low Affinity Aromatic-preferring Amino Acid Transporter (arpAT)

Fernández, Esperanza; Torrents, David; Zorzano, António; Palacı́n, Manuel; Chillarón, Josep

doi:10.1074/jbc.m412516200

Cited by 22 publications

(11 citation statements)

References 64 publications

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“…The immediate precursors of DA and serotonin are apparently captured to monoenzymatic AADC neurons by a membrane transporter of large neutral amino acids that is an attribute of different cells including neurons (Ferná ndez et al, 2005). DA synthesis in monoenzymatic AADC neurons is manifested by an intraneuronal accumulation of DA after the L-DOPA administration.…”

Section: Monoenzymatic Aadc Neuronsmentioning

confidence: 99%

Non-dopaminergic neurons partly expressing dopaminergic phenotype: Distribution in the brain, development and functional significance

Ugrumov

2009

Journal of Chemical Neuroanatomy

114

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Section: Monoenzymatic Aadc Neuronsmentioning

confidence: 99%

Non-dopaminergic neurons partly expressing dopaminergic phenotype: Distribution in the brain, development and functional significance

Ugrumov

2009

Journal of Chemical Neuroanatomy

114

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“…Six of these light subunits heterodimerize with 4F2hc (LAT1, LAT2, y + LAT1, y + LAT2, asc1 and xCT) [4][5][6][7][8][9], two with rBAT (b 0, + AT and AGT1) [10,11]. For two [arpAT (SLC7A15) and asc2 (SLC7A12), not present in primates] [12,13], the heavy subunit has not been identified ( Table 1).…”

Section: Introductionmentioning

confidence: 91%

Heteromeric amino acid transporters. In search of the molecular bases of transport cycle mechanisms

Palacı́n

Errasti-Murugarren

Rosell

2016

Biochemical Society Transactions

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Heteromeric amino acid transporters (HATs) are relevant targets for structural studies. On the one hand, HATs are involved in inherited and acquired human pathologies. On the other hand, these molecules are the only known examples of solute transporters composed of two subunits (heavy and light) linked by a disulfide bridge. Unfortunately, structural knowledge of HATs is scarce and limited to the atomic structure of the ectodomain of a heavy subunit (human 4F2hc-ED) and distant prokaryotic homologues of the light subunits that share a LeuT-fold. Recent data on human 4F2hc/LAT2 at nanometer resolution revealed 4F2hc-ED positioned on top of the external loops of the light subunit LAT2. Improved resolution of the structure of HATs, combined with conformational studies, is essential to establish the structural bases for light subunit recognition and to evaluate the functional relevance of heavy and light subunit interactions for the amino acid transport cycle.

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“…When the amino acid substrate preferences of the different members of the SLC7 family are considered, it is unlikely that human transporters other than LAT1 and LAT2 facilitate the cellular uptake of iodothyronines; however, a new member of this family, aromatic-preferring amino acid transporter (arpAT), has been cloned very recently from mice but is not expressed in humans [69]. ArpAT is capable of heterodimerizing with both rBAT and 4F2hc, and, as its name indicates, shows a preference for aromatic amino acids.…”

Section: Amino Acid Transportersmentioning

confidence: 99%

Membrane transporters for thyroid hormone

Friesema

Jansen

Visser

2005

Current Opinion in Endocrinology & Diabetes

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Purpose of reviewAction and metabolism of thyroid hormones are intracellular events, which require their uptake across the plasma membrane. Cellular uptake of thyroid hormone is mediated by transporters, and recently, some of these transporters have been identified at the molecular level. Here we review the biochemistry, molecular biology, and clinical relevance of these transporters. Recent findingsIodothyronine transporters have been identified among the members of different transporter families, including Na/taurocholate cotransporting polypeptide, different (Na-independent) organic anion transporting polypeptides, the L-type amino acid transporters, and monocarboxylate transporter-8. Two transporters are particularly interesting: organic anion transporting polypeptide-1C1, which shows a high affinity for T4 and T3 and is almost exclusively expressed in brain, and monocarboxylate transporter-8, which is a very active iodothyronine transporter with a slight preference for T3 and is abundantly expressed in different tissues, including brain. Organic anion transporting polypeptide-1C1 is probably important for T4 transport across the blood--brain barrier and that monocarboxylate transporter-8 for T3 uptake in neurons. Recently, mutations in MCT8, which is located on the X chromosome, were identified in male patients with severe psychomotor retardation and elevated serum levels of T3. Summary Recent studies have greatly increased our knowledge about the identity of thyroid hormone transporters and in particular their physiologic relevance. The dramatic consequences of mutations in monocarboxylate transporter-8 represent a novel mechanism of thyroid hormone resistance due to inhibited cellular entry of the hormone.

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Identification and Functional Characterization of a Novel Low Affinity Aromatic-preferring Amino Acid Transporter (arpAT)

Cited by 22 publications

References 64 publications

Non-dopaminergic neurons partly expressing dopaminergic phenotype: Distribution in the brain, development and functional significance

Non-dopaminergic neurons partly expressing dopaminergic phenotype: Distribution in the brain, development and functional significance

Heteromeric amino acid transporters. In search of the molecular bases of transport cycle mechanisms

Membrane transporters for thyroid hormone

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