Molecular Ontology of Amino Acid Transport

Boudko, Dmitri Y.

doi:10.1007/978-1-60327-229-2_16

Cited by 9 publications

(16 citation statements)

References 409 publications

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“…NATs, paralogous to those present in Bacteria and Archaea, tend to form species-specific clusters in different animal clades. Moreover, NATs appear to be much more diverse in substrate specificity compared with NTTs (Boudko, 2010). Previous studies have shown that NATs are broadly and universally involved in the alimentary absorption and distribution of essential amino acids across different metazoan organisms and tissues (Boudko et al, 2005a;Boudko et al, 2005b 2 ) in at least three different plates.…”

Section: Discussionmentioning

confidence: 99%

“…However, the substrates of this transporter remain unknown. Phylogenomic trees of the SLC6 family including nematode representatives have been published previously (Boudko et al, 2005a;Meleshkevitch et al, 2009b;Boudko, 2010;Dierking et al, 2011). The phylogenomic analysis presented in this work focuses on identification of NAT homologs and includes additional nematode species.…”

Section: Phylogenymentioning

confidence: 99%

“…Except for some specific additions, it includes ~50% of the proteinogenic amino acids that utilize complex synthesis cascades that consume the lion's share of the total energy budget in autotrophic bacteria and plants (Payne and Loomis, 2006;Boudko, 2010). The heterotrophy of these amino acids accelerates development and reproduction in animals by reducing the energy and time necessary to synthesize amino acids, peptides and proteins.…”

Section: Introductionmentioning

confidence: 99%

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A SLC6 transporter of the novel B0,- system aids in absorption and detection of nutrient amino acids in Caenorhabditis elegans

Metzler

Meleshkevitch

Fox

et al. 2013

Journal of Experimental Biology

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Summary Nutrient Amino acid Transporters (NATs) of SoLute Carrier family 6 (SLC6) mediate uptake of essential amino acids in mammals and insects. Phylogenomic analysis of the Caenorhabditis elegans (Ce) SLC6 family identifies 5 genes paralogous to an insect-specific NAT subfamily. Here we cloned and characterized the first representative of the identified nematode-specific transporters, SNF-5. SNF-5 mediates broad spectrum cation-coupled transport of neutral amino acids with submillimolar affinities and stoichiometry of 1AA:1Na+, except for 1L-Pro:2 Na+. Unexpectedly, it transports acidic L-Glu- and L-Asp- (AA -1:3Na+), revealing it to be the first member of a new B0,- system among characterized SLC6 transporters. This activity correlates with a unique positively charged His+ 377 in the substrate-binding pocket. snf-5 promoter-driven EGFP labels intestinal cells INT1-9 and three pairs of amphid sensory neurons: ASI, ADF, and ASK. These cells are intimately involved in control of dauer diapause, development, metabolism, and longevity. The snf-5 deletion mutants do not show apparent morphological disorders, but increase dauer formation while reducing dauer maintenance upon starvation. Overall, our studies characterized the first nematode-specific NAT and revealed important structural and functional aspects of this transporter. In addition to the predictable role in alimentary amino acid absorption, our results indicate possible neuronal roles of SNF-5 as an amino acid provider to specific neuronal functions, including sensing of amino acid availability.

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Section: Discussionmentioning

confidence: 99%

Section: Phylogenymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A SLC6 transporter of the novel B0,- system aids in absorption and detection of nutrient amino acids in Caenorhabditis elegans

Metzler

Meleshkevitch

Fox

et al. 2013

Journal of Experimental Biology

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“…In eukaryotic cells, amino acid absorption is mediated exclusively by secondary transporters, which are divided on active or ion electrochemical-energy-coupled symporter mechanisms (also termed as electrogenic or, more appropriately, electrophoretic), exchangers that could have active and passive components but cannot perform significant accumulative transport, and passive uniporters that facilitate membrane transport of amino acids down a chemical gradient (Wolfersberger, 1994). Phylogenetic analysis identifies ~50 families of secondary transporters (Hediger et al, 2004), 10 of which contribute at least one member to the transport of amino acids or their metabolized derivatives (Boudko, 2010; Boudko et al, 2005b). These families have been summarized in the Transporter Classification Data Base (TCDB) (Busch and Saier, 2003; Saier, 1999, 2000) and the SoLute Carrier family systematics (Hediger et al, 2004) (SLC; originally proposed by the Human Genome Organization (HUGO) Nomenclature Committee).…”

Section: Molecular Specificity and Diversity Of The Metazoan Aminomentioning

confidence: 99%

“…The rest of these genes encode alternative transporters for amino acid derived metabolites, transport other organic and inorganic solutes, mediate signaling functions without apparent transport, or denote remains of transporter evolution, pseudo genes. The SLC1, 32, 36, and 38 families, with limited inferred roles in the transport of essential amino acids, were previously summarized (Boudko, 2010; Boudko et al, 2005b). SLC15 members have been characterized as proton driven oligopeptide and histidine transporters in the mammalian alimentary canal and other tissues (Boll et al, 1996; Daniel and Kottra, 2003).…”

Section: Amino Acid Transporters In Insectsmentioning

confidence: 99%

Molecular basis of essential amino acid transport from studies of insect nutrient amino acid transporters of the SLC6 family (NAT-SLC6)

Boudko

2012

Journal of Insect Physiology

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Two protein families that represent major components of essential amino acid transport in insects have been identified. They are annotated as the SLC6 and SLC7 families of transporters according to phylogenetic proximity to characterized amino acid transporters (HUGO nomenclature). Members of these families have been identified as important apical and basolateral parts of transepithelial essential amino acid absorption in the metazoan alimentary canal. Synergistically, they play critical physiological roles as essential substrate providers to diverse metabolic processes, including generic protein synthesis. This review briefly clarifies the requirements for amino acid transport and a variety of amino acid transport mechanisms, including the aforementioned families. Further it focuses on the large group of Nutrient Amino acid Transporters (NATs), which comprise a recently identified subfamily of the Neurotransmitter Sodium Symporter family (NSS or SLC6). The first insect NAT, cloned from the caterpillar gut, has a broad substrate spectrum similar to mammalian B0 transporters. Several new NAT-SLC6 members have been characterized in an effort to explore mechanisms for the essential amino acid absorption in model dipteran insects. The identification and functional characterization of new B0-like and narrow specificity transporters of essential amino acids in fruit fly and mosquitoes leads to a fundamentally important insight: that NATs evolved and act together as the integrated active core of a transport network that mediates active alimentary absorption and systemic distribution of essential amino acids. This role of NATs is projected from the most primitive prokaryotes to the most complex metazoan organisms, and represents an interesting platform for unraveling the molecular evolution of amino acid transport and modeling amino acid transport disorders. The comparative study of NATs elucidates important adaptive differences between essential amino acid transportomes of invertebrate and vertebrate organisms, outlining a new possibility for selective targeting of essential amino acid absorption mechanisms to control medically and economically important arthropods and other invertebrate organisms.

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Free d-Aspartate in Nonmammalian Animals: Detection, Localization, Metabolism, and Function

et al. 2016

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Molecular Ontology of Amino Acid Transport

Cited by 9 publications

References 409 publications

A SLC6 transporter of the novel B0,- system aids in absorption and detection of nutrient amino acids in Caenorhabditis elegans

A SLC6 transporter of the novel B0,- system aids in absorption and detection of nutrient amino acids in Caenorhabditis elegans

Molecular basis of essential amino acid transport from studies of insect nutrient amino acid transporters of the SLC6 family (NAT-SLC6)

Free d-Aspartate in Nonmammalian Animals: Detection, Localization, Metabolism, and Function

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