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  1. Article: Heteromeric amino acid transporters: biochemistry, genetics, and physiology.

    Chillarón, J / Roca, R / Valencia, A / Zorzano, A / Palacín, M

    American journal of physiology. Renal physiology

    2001  Volume 281, Issue 6, Page(s) F995–1018

    Abstract: ... activation. This review covers the biochemistry, human genetics, and cell physiology of HATs, including ... The heteromeric amino acid transporters (HATs) are composed of two polypeptides: a heavy subunit ... mammalian amino acid transport systems (e.g., L isoforms, y(+)L isoforms, asc, x(c)(-), and b(0,+)). Members ...

    Abstract The heteromeric amino acid transporters (HATs) are composed of two polypeptides: a heavy subunit (HSHAT) and a light subunit (LSHAT) linked by a disulfide bridge. HSHATs are N-glycosylated type II membrane glycoproteins, whereas LSHATs are nonglycosylated polytopic membrane proteins. The HSHATs have been known since 1992, and the LSHATs have been described in the last three years. HATs represent several of the classic mammalian amino acid transport systems (e.g., L isoforms, y(+)L isoforms, asc, x(c)(-), and b(0,+)). Members of the HAT family are the molecular bases of inherited primary aminoacidurias cystinuria and lysinuric protein intolerance. In addition to the role in amino acid transport, one HSHAT [the heavy subunit of the cell-surface antigen 4F2 (also named CD98)] is involved in other cell functions that might be related to integrin activation. This review covers the biochemistry, human genetics, and cell physiology of HATs, including the multifunctional character of CD98.
    MeSH term(s) Amino Acid Sequence ; Amino Acid Transport Systems/chemistry ; Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/physiology ; Animals ; Biological Transport ; Fusion Regulatory Protein-1/physiology ; Humans ; Integrins/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Neoplasms/etiology ; Renal Aminoacidurias/etiology ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
    Chemical Substances Amino Acid Transport Systems ; Fusion Regulatory Protein-1 ; Integrins
    Language English
    Publishing date 2001-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 603837-2
    ISSN 1522-1466 ; 1931-857X ; 0363-6127
    ISSN (online) 1522-1466
    ISSN 1931-857X ; 0363-6127
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  2. Article ; Online: Heteromeric amino acid transporters. In search of the molecular bases of transport cycle mechanisms.

    Palacín, Manuel / Errasti-Murugarren, Ekaitz / Rosell, Albert

    Biochemical Society transactions

    2016  Volume 44, Issue 3, Page(s) 745–752

    Abstract: Heteromeric amino acid transporters (HATs) are relevant targets for structural studies. On the one ... for the amino acid transport cycle. ... are the only known examples of solute transporters composed of two subunits (heavy and light) linked ...

    Abstract 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.
    MeSH term(s) Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Amino Acid Transport Systems/physiology ; Animals ; Bacteria/metabolism ; Catalytic Domain ; Genes ; Humans ; Protein Conformation
    Chemical Substances Amino Acid Transport Systems
    Language English
    Publishing date 2016-06-15
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20150294
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  3. Article: The structural and functional units of heteromeric amino acid transporters. The heavy subunit rBAT dictates oligomerization of the heteromeric amino acid transporters.

    Fernández, Esperanza / Jiménez-Vidal, Maite / Calvo, María / Zorzano, Antonio / Tebar, Francesc / Palacín, Manuel / Chillarón, Josep

    The Journal of biological chemistry

    2006  Volume 281, Issue 36, Page(s) 26552–26561

    Abstract: Heteromeric amino acid transporters are composed of a catalytic light subunit and a heavy subunit ... linked by a disulfide bridge. We analyzed the structural and functional units of systems b0,+ and xC ... formed by the heterodimers b0,+ AT-rBAT and xCT-4F2hc, respectively. Blue Native gel electrophoresis ...

    Abstract Heteromeric amino acid transporters are composed of a catalytic light subunit and a heavy subunit linked by a disulfide bridge. We analyzed the structural and functional units of systems b0,+ and xC-, formed by the heterodimers b0,+ AT-rBAT and xCT-4F2hc, respectively. Blue Native gel electrophoresis, cross-linking, and fluorescence resonance energy transfer in vivo indicate that system b0,+ is a heterotetramer [b0,+ AT-rBAT]2, whereas xCT-4F2hc seems not to stably or efficiently oligomerize. However, substitution of the heavy subunit 4F2hc for rBAT was sufficient to form a heterotetrameric [xCT-rBAT]2 structure. The functional expression of concatamers of two light subunits (which differ only in their sensitivity to inactivation by a sulfhydryl reagent) suggests that a single heterodimer is the functional unit of systems b0,+ and xC-.
    MeSH term(s) Amino Acid Transport Systems/chemistry ; Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Animals ; Dimerization ; Fluorescence Resonance Energy Transfer ; Fusion Regulatory Protein 1, Heavy Chain/genetics ; Fusion Regulatory Protein 1, Heavy Chain/metabolism ; HeLa Cells ; Humans ; Luminescent Proteins/metabolism ; Mice ; Oocytes/cytology ; Oocytes/physiology ; Protein Structure, Quaternary ; Protein Subunits/chemistry ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Xenopus laevis
    Chemical Substances Amino Acid Transport Systems ; Fusion Regulatory Protein 1, Heavy Chain ; Luminescent Proteins ; Protein Subunits ; Recombinant Fusion Proteins
    Language English
    Publishing date 2006-07-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M604049200
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  4. Article ; Online: Exon-skipping splice variants of excitatory amino acid transporter-2 (EAAT2) form heteromeric complexes with full-length EAAT2.

    Gebhardt, Florian M / Mitrovic, Ann D / Gilbert, Daniel F / Vandenberg, Robert J / Lynch, Joseph W / Dodd, Peter R

    The Journal of biological chemistry

    2010  Volume 285, Issue 41, Page(s) 31313–31324

    Abstract: The glial transporter excitatory amino acid transporter-2 (EAAT2) is the main mediator of glutamate ... in which each protomer functions autonomously. Several EAAT2 variants are found in control and Alzheimer-diseased human ... the exon-7 deletion variant was not trafficked to the membrane when transfected alone, and ...

    Abstract The glial transporter excitatory amino acid transporter-2 (EAAT2) is the main mediator of glutamate clearance in brain. The wild-type transporter (EAAT2wt) forms trimeric membrane complexes in which each protomer functions autonomously. Several EAAT2 variants are found in control and Alzheimer-diseased human brains; their expression increases with pathological severity. These variants might alter EAAT2wt-mediated transport by abrogating membrane trafficking, or by changing the configuration or functionality of the assembled transporter complex. HEK293 cells were transfected with EAAT2wt; EAAT2b, a C-terminal variant; or either of two exon-skipping variants: alone or in combination. Surface biotinylation studies showed that only the exon-7 deletion variant was not trafficked to the membrane when transfected alone, and that all variants could reach the membrane when co-transfected with EAAT2wt. Fluorescence resonance energy transfer (FRET) studies showed that co-transfected EAAT2wt and EAAT2 splice variants were expressed in close proximity. Glutamate transporter function was measured using a whole cell patch clamp technique, or by changes in membrane potential indexed by a voltage-sensitive fluorescent dye (FMP assay): the two methods gave comparable results. Cells transfected with EAAT2wt or EAAT2b showed glutamate-dependent membrane potential changes consistent with functional expression. Cells transfected with EAAT2 exon-skipping variants alone gave no response to glutamate. Co-transfection of EAAT2wt (or EAAT2b) and splice variants in various ratios significantly raised glutamate EC(50) and decreased Hill coefficients. We conclude that exon-skipping variants form heteromeric complexes with EAAT2wt or EAAT2b that traffic to the membrane but show reduced glutamate-dependent activity. This could allow glutamate to accumulate extracellularly and promote excitotoxicity.
    MeSH term(s) Alternative Splicing ; Base Sequence ; Cell Line ; Excitatory Amino Acid Transporter 2 ; Exons/physiology ; Glutamate Plasma Membrane Transport Proteins/genetics ; Glutamate Plasma Membrane Transport Proteins/metabolism ; Glutamic Acid/genetics ; Glutamic Acid/metabolism ; Humans ; Membrane Potentials/physiology ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Transport/physiology ; Sequence Deletion
    Chemical Substances Excitatory Amino Acid Transporter 2 ; Glutamate Plasma Membrane Transport Proteins ; Multiprotein Complexes ; Protein Isoforms ; SLC1A2 protein, human ; Glutamic Acid (3KX376GY7L)
    Language English
    Publishing date 2010-08-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M110.153494
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  5. Article: Different domains regulate homomeric and heteromeric complex formation among type I and type II transforming growth factor-beta receptors.

    Rechtman, Maya Mouler / Nakaryakov, Alex / Shapira, Keren E / Ehrlich, Marcelo / Henis, Yoav I

    The Journal of biological chemistry

    2009  Volume 284, Issue 12, Page(s) 7843–7852

    Abstract: ... The homodimerization of TbetaRII depends on a cytoplasmic juxtamembrane region (amino acid residues 200-220 ... Transforming growth factor-beta (TGF-beta) binds to and signals via two serine-threonine kinase ... receptors, type I (TbetaRI) and type II (TbetaRII). The oligomerization of TGF-beta receptors modulates ...

    Abstract Transforming growth factor-beta (TGF-beta) binds to and signals via two serine-threonine kinase receptors, type I (TbetaRI) and type II (TbetaRII). The oligomerization of TGF-beta receptors modulates ligand binding and receptor trafficking and may contribute to signal diversification. However, numerous features of the molecular domains that determine the homo- and hetero-oligomerization of full-length receptors at the cell surface and the mode of these interactions remain unclear. Here, we address these questions through computerized immunofluorescence co-patching and patch/fluorescence recovery after photobleaching measurements of different combinations of epitope-tagged receptors and their mutants in live cells. We show that TbetaRI and TbetaRII are present on the plasma membrane both as monomers and homo- and hetero-oligomers. The homodimerization of TbetaRII depends on a cytoplasmic juxtamembrane region (amino acid residues 200-220). In contrast, the cytoplasmic domain of TbetaRI is dispensable for its homodimerization. TbetaRI.TbetaRII hetero-oligomerization depends on the cytoplasmic domain of TbetaRI and on a C-terminal region of TbetaRII (residues 419-565). TGF-beta1 elevates TbetaRII homodimerization to some degree and strongly enhances TbetaRI.TbetaRII heteromeric complex formation. Both ligand-induced effects depend on the region encompassed between residues 200-242 of TbetaRII. Furthermore, the kinase activity of TbetaRI is also necessary for the latter effect. All forms of the homo- and hetero-oligomers, whether constitutively present on the membrane or formed upon TGF-beta1 stimulation, were stable in the time-scale of our patch/FRAP measurements. We suggest that the different forms of receptor oligomerization may serve as a basis for the heterogeneity of TGF-beta signaling responses.
    MeSH term(s) Animals ; COS Cells ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Chlorocebus aethiops ; Dimerization ; Humans ; Ligands ; Photobleaching ; Protein Binding/physiology ; Protein Structure, Tertiary/physiology ; Protein Transport/physiology ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Receptor, Transforming Growth Factor-beta Type I ; Receptor, Transforming Growth Factor-beta Type II ; Receptors, Transforming Growth Factor beta/genetics ; Receptors, Transforming Growth Factor beta/metabolism ; Signal Transduction/physiology ; Transforming Growth Factor beta1/genetics ; Transforming Growth Factor beta1/metabolism
    Chemical Substances Ligands ; Receptors, Transforming Growth Factor beta ; Transforming Growth Factor beta1 ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Receptor, Transforming Growth Factor-beta Type I (EC 2.7.11.30) ; Receptor, Transforming Growth Factor-beta Type II (EC 2.7.11.30)
    Language English
    Publishing date 2009-01-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M809215200
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  6. Article: Existence and theoretical aspects of homomeric and heteromeric dopamine receptor complexes and their relevance for neurological diseases.

    Agnati, Luigi Francesco / Ferre, Sergi / Burioni, Raffaella / Woods, Amina / Genedani, Susanna / Franco, Rafael / Fuxe, Kjell

    Neuromolecular medicine

    2005  Volume 7, Issue 1-2, Page(s) 61–78

    Abstract: ... mGluR5, N-methyl-D-aspartate (NMDA), gamma-aminobutryic acid (GABA)-A, and alpha-amino-3-hydroxy-5-methyl ... in physiological and pathological conditions are discussed. The effects of temperature on RM are discussed not only ... inward rectifying potassium channels and dopamine transporter activity. Also, ligand-gated ion channels such as GABA-A and NMDA ...

    Abstract Dopamine (DA) and other receptors physically interact in the plasma membrane of basal ganglia neurons forming receptor mosaics (RMs). Two types of RMs are discussed, homomers formed only by DA-receptor (DA-R) subtypes and heteromers formed by DA-R associated with other receptors, such as A2A, A1, mGluR5, N-methyl-D-aspartate (NMDA), gamma-aminobutryic acid (GABA)-A, and alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid. By being part of horizontal molecular networks, RMs tune multiple effector systems already at membrane level, such as G protein regulated inward rectifying potassium channels and dopamine transporter activity. Also, ligand-gated ion channels such as GABA-A and NMDA receptors are modulated by DA-R, e.g., in the striatal GABA output neurons through the formation of heteromeric complexes with these receptors. Thus, intramembrane DA-R-receptor interactions play an important role in the information handling in the basal ganglia. On this basis, functional implications of DA RM in physiological and pathological conditions are discussed. The effects of temperature on RM are discussed not only because receptor-decoding mechanisms are temperature sensitive, but also in view of the suggestion that possible ordering effects (i.e., changes in the entropy of a receptor complex) induced by a ligand are as a result of alterations in the receptor oligomerization (i.e., are related to rearrangements of the RM). Hence, brain temperature may have profound effects on brain integrative functions not only because its effects on the kinetics of biochemical reactions, but also for its effects on receptor geometry, building up of RM, and alterations in protein expression, as is the case of H-channels following febrile seizures.
    MeSH term(s) Animals ; Basal Ganglia/metabolism ; Basal Ganglia/physiopathology ; Basal Ganglia Diseases/genetics ; Basal Ganglia Diseases/metabolism ; Basal Ganglia Diseases/physiopathology ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Humans ; Ion Channels/chemistry ; Ion Channels/metabolism ; Macromolecular Substances/chemistry ; Macromolecular Substances/metabolism ; Neurons/metabolism ; Receptor Cross-Talk/physiology ; Receptors, Dopamine/chemistry ; Receptors, Dopamine/metabolism ; Receptors, Glutamate/chemistry ; Receptors, Glutamate/metabolism
    Chemical Substances Ion Channels ; Macromolecular Substances ; Receptors, Dopamine ; Receptors, Glutamate
    Language English
    Publishing date 2005
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2077809-0
    ISSN 1559-1174 ; 1535-1084
    ISSN (online) 1559-1174
    ISSN 1535-1084
    DOI 10.1385/NMM:7:1-2:061
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  7. Article: Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes.

    Noureddine, Hiba / Schmitt, Claudine / Liu, Wangqing / Garbay, Christiane / Massoulié, Jean / Bon, Suzanne

    The Journal of biological chemistry

    2006  Volume 282, Issue 6, Page(s) 3487–3497

    Abstract: ... without its transmembrane and cytoplasmic domains (P(stp54) mutant), produced secreted heteromeric complexes (T4-P(stp54 ... and secretion of a heteromeric complex with four AChE(T) subunits, nearly as efficiently as the entire ... motif (14 prolines with an intervening leucine, P4LP10), a transmembrane domain, and a cytoplasmic ...

    Abstract The membrane-bound form of acetylcholinesterase (AChE) constitutes the major component of this enzyme in the mammalian brain. These molecules are hetero-oligomers, composed of four AChE catalytic subunits of type T (AChE(T)), associated with a transmembrane protein of type 1, called PRiMA (proline-rich membrane anchor). PRiMA consists of a signal peptide, an extracellular domain that contains a proline-rich motif (14 prolines with an intervening leucine, P4LP10), a transmembrane domain, and a cytoplasmic domain. Expression of AChE(T) subunits in transfected COS cells with a truncated PRiMA, without its transmembrane and cytoplasmic domains (P(stp54) mutant), produced secreted heteromeric complexes (T4-P(stp54)), instead of membrane-bound tetramers. In this study, we used a series of deletions and point mutations to analyze the interaction between the extracellular domain of PRiMA and AChE(T) subunits. We confirmed the importance of the polyproline stretches and defined a peptidic motif (RP4LP10RL), which induces the assembly and secretion of a heteromeric complex with four AChE(T) subunits, nearly as efficiently as the entire extracellular domain of PRiMA. It is noteworthy that deletion of the N-terminal segment preceding the prolines had little effect. Interestingly, short PRiMA mutants, truncated within the proline-rich motif, reduced both cellular and secreted AChE activity, suggesting that their interaction with AChE(T) subunits induces their intracellular degradation.
    MeSH term(s) Acetylcholinesterase/chemistry ; Acetylcholinesterase/metabolism ; Acetylcholinesterase/physiology ; Amino Acid Motifs/genetics ; Amino Acid Sequence ; Animals ; COS Cells ; Catalytic Domain/genetics ; Chlorocebus aethiops ; Cricetinae ; Extracellular Space/chemistry ; Extracellular Space/genetics ; Extracellular Space/physiology ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Membrane Proteins/physiology ; Mice ; Molecular Sequence Data ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Multiprotein Complexes/physiology ; Mutagenesis, Site-Directed ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/physiology ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Peptides/physiology ; Protein Transport/genetics ; Rats ; Sequence Deletion/genetics ; Signal Transduction/genetics
    Chemical Substances Membrane Proteins ; Multiprotein Complexes ; Nerve Tissue Proteins ; PRiMA1 protein, rat ; Peptides ; prima1 protein, mouse ; Acetylcholinesterase (EC 3.1.1.7)
    Language English
    Publishing date 2006-12-08
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M607221200
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  8. Article ; Online: The four major N- and C-terminal splice variants of the excitatory amino acid transporter GLT-1 form cell surface homomeric and heteromeric assemblies.

    Peacey, Eleanor / Miller, Christopher C J / Dunlop, John / Rattray, Marcus

    Molecular pharmacology

    2009  Volume 75, Issue 5, Page(s) 1062–1073

    Abstract: ... of the excitatory amino acid transporter (EAAT) family that controls extracellular L-glutamate levels and is important ... MAST-DIETCI, and MPK-DIETCI according to amino acid sequence) in a range of cell lines and primary ... degraded. This study provides direct biochemical evidence for oligomeric assembly of GLT-1 and reports ...

    Abstract The L-glutamate transporter GLT-1 is an abundant central nervous system (CNS) membrane protein of the excitatory amino acid transporter (EAAT) family that controls extracellular L-glutamate levels and is important in limiting excitotoxic neuronal death. Using reverse transcription-polymerase chain reaction, we have determined that four mRNAs encoding GLT-1 exist in mouse brain, with the potential to encode four GLT-1 isoforms that differ in their N and C termini. We expressed all four isoforms (termed MAST-KREK, MPK-KREK, MAST-DIETCI, and MPK-DIETCI according to amino acid sequence) in a range of cell lines and primary astrocytes and show that each isoform can reach the cell surface. In transfected human embryonic kidney (HEK) 293 or COS-7 cells, all four isoforms support high-affinity sodium-dependent L-glutamate uptake with identical pharmacological and kinetic properties. Inserting a viral epitope (tagged with V5, hemagglutinin, or FLAG) into the second extracellular domain of each isoform allowed coimmunoprecipitation and time-resolved Förster resonance energy transfer (tr-FRET) studies using transfected HEK-293 cells. Here we show for the first time that each of the four isoforms is able to combine to form homomeric and heteromeric assemblies, each of which is expressed at the cell surface of primary astrocytes. After activation of protein kinase C by phorbol ester, V5-tagged GLT-1 is rapidly removed from the cell surface of HEK-293 cells and degraded. This study provides direct biochemical evidence for oligomeric assembly of GLT-1 and reports the development of novel tools to provide insight into the trafficking of GLT-1.
    MeSH term(s) Animals ; Cells, Cultured ; Excitatory Amino Acid Transporter 2/chemistry ; Excitatory Amino Acid Transporter 2/genetics ; Excitatory Amino Acid Transporter 2/physiology ; Humans ; Mice ; Protein Isoforms ; Protein Kinase C/physiology ; Tetradecanoylphorbol Acetate/pharmacology
    Chemical Substances Excitatory Amino Acid Transporter 2 ; Protein Isoforms ; Protein Kinase C (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
    Language English
    Publishing date 2009-02-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 124034-1
    ISSN 1521-0111 ; 0026-895X
    ISSN (online) 1521-0111
    ISSN 0026-895X
    DOI 10.1124/mol.108.052829
    Database MEDical Literature Analysis and Retrieval System OnLINE

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