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Volumn 8, Issue 3, 1998, Pages 405-412

Vesicular neurotransmitter transport and the presynaptic regulation of quantal size

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; ACETYLCHOLINE; MONOAMINE; NEUROTRANSMITTER; PROTEIN;

EID: 0032104055     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(98)80068-8     Document Type: Article
Times cited : (100)

References (44)
  • 1
    • 0028912433 scopus 로고
    • Vesicular neurotransmitter transporters: From bacteria to humans
    • Schuldiner S, Shirvan A, Linial M. Vesicular neurotransmitter transporters: from bacteria to humans. Physiol Rev. 75:1995;369-392.
    • (1995) Physiol Rev , vol.75 , pp. 369-392
    • Schuldiner, S.1    Shirvan, A.2    Linial, M.3
  • 2
    • 0031044233 scopus 로고    scopus 로고
    • The role of vesicular transport proteins in synaptic transmission and neural degeneration
    • Liu Y, Edwards RH. The role of vesicular transport proteins in synaptic transmission and neural degeneration. Annu Rev Neurosci. 20:1997;125-156.
    • (1997) Annu Rev Neurosci , vol.20 , pp. 125-156
    • Liu, Y.1    Edwards, R.H.2
  • 3
    • 0019877702 scopus 로고
    • +-linked dopamine transport in chromaffin granule ghosts
    • +-linked dopamine transport in chromaffin granule ghosts. Biochemistry. 20:1981;6625-6629.
    • (1981) Biochemistry , vol.20 , pp. 6625-6629
    • Knoth, J.1    Zallakian, M.2    Njus, D.3
  • 4
    • 0023715532 scopus 로고
    • Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes
    • Maycox PR, Deckwerth T, Hell JW, Jahn R. Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes. J Biol Chem. 263:1988;15423-15428.
    • (1988) J Biol Chem , vol.263 , pp. 15423-15428
    • Maycox, P.R.1    Deckwerth, T.2    Hell, J.W.3    Jahn, R.4
  • 5
    • 0024550284 scopus 로고
    • Characterization of the solubilized and reconstituted ATP-dependent vesicular glutamate uptake system
    • Carlson MD, Kish PE, Ueda T. Characterization of the solubilized and reconstituted ATP-dependent vesicular glutamate uptake system. J Biol Chem. 264:1989;7369-7376.
    • (1989) J Biol Chem , vol.264 , pp. 7369-7376
    • Carlson, M.D.1    Kish, P.E.2    Ueda, T.3
  • 6
    • 0025041769 scopus 로고
    • Energy dependence and functional reconstitution of the gamma-aminobutyric acid carrier from synaptic vesicles
    • Hell JW, Maycox PR, Jahn R. Energy dependence and functional reconstitution of the gamma-aminobutyric acid carrier from synaptic vesicles. J Biol Chem. 265:1990;2111-2117.
    • (1990) J Biol Chem , vol.265 , pp. 2111-2117
    • Hell, J.W.1    Maycox, P.R.2    Jahn, R.3
  • 7
    • 0025647857 scopus 로고
    • Amphetamine and other psychostimulants reduce pH gradients in midbrain dopaminergic neurons and chromaffin granules: A mechanism of action
    • Sulzer D, Rayport S. Amphetamine and other psychostimulants reduce pH gradients in midbrain dopaminergic neurons and chromaffin granules: a mechanism of action. Neuron. 5:1990;797-808.
    • (1990) Neuron , vol.5 , pp. 797-808
    • Sulzer, D.1    Rayport, S.2
  • 8
    • 0026756443 scopus 로고
    • Gene transfer of a reserpine-sensitive mechanism of resistance to MPP+
    • Liu Y, Roghani A, Edwards RH. Gene transfer of a reserpine-sensitive mechanism of resistance to MPP+. Proc Natl Acad Sci USA. 89:1992;9074-9078.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9074-9078
    • Liu, Y.1    Roghani, A.2    Edwards, R.H.3
  • 10
    • 0026458380 scopus 로고
    • Expression cloning of a reserpine-sensitive vesicular monoamine transporter
    • Erickson JD, Eiden LE, Hoffman BJ. Expression cloning of a reserpine-sensitive vesicular monoamine transporter. Proc Natl Acad Sci USA. 89:1992;10993-10997.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10993-10997
    • Erickson, J.D.1    Eiden, L.E.2    Hoffman, B.J.3
  • 11
    • 0027274981 scopus 로고
    • The Caenorhabditis elegans unc-17 gene: A putative vesicular acetylcholine transporter
    • Alfonso A, Grundahl K, Duerr JS, Han H-P, Rand JB. The Caenorhabditis elegans unc-17 gene: a putative vesicular acetylcholine transporter. Science. 261:1993;617-619.
    • (1993) Science , vol.261 , pp. 617-619
    • Alfonso, A.1    Grundahl, K.2    Duerr, J.S.3    Han H-P4    Rand, J.B.5
  • 14
    • 0030709324 scopus 로고    scopus 로고
    • Differential localization of vesicular acetylcholine and monoamine transporters in PC12 cells but not CHO cells
    • of special interest. This report documents the differential localization of VMATs and VAChT in PC12 cells that was suggested by Bauerfeind et al. 1993 [33]. VMATs localize preferentially to LDCVs whereas VAChT localizes preferentially to light vesicles, including SLMVs, in PC12 cells.
    • Liu Y, Edwards RH. Differential localization of vesicular acetylcholine and monoamine transporters in PC12 cells but not CHO cells. of special interest J Cell Biol. 139:1997;907-916 This report documents the differential localization of VMATs and VAChT in PC12 cells that was suggested by Bauerfeind et al. 1993 [33]. VMATs localize preferentially to LDCVs whereas VAChT localizes preferentially to light vesicles, including SLMVs, in PC12 cells.
    • (1997) J Cell Biol , vol.139 , pp. 907-916
    • Liu, Y.1    Edwards, R.H.2
  • 15
    • 0029861246 scopus 로고    scopus 로고
    • Active transport of acetylcholine by the human vesicular acetylcholine transporter
    • Varoqui H, Erickson JD. Active transport of acetylcholine by the human vesicular acetylcholine transporter. J Biol Chem. 271:1996;27229-27232.
    • (1996) J Biol Chem , vol.271 , pp. 27229-27232
    • Varoqui, H.1    Erickson, J.D.2
  • 16
    • 0030968854 scopus 로고    scopus 로고
    • Expression of putative vesicular acetylcholine transporter facilitates quantal transmitter packaging
    • of outstanding interest. Using a Xenopus culture system in which motor neurons form synapses with muscle cells, expression of VAChT in the motor neurons but not the muscle cells increases quantal size, indicating that the transporter can limit the rate of SV filling. VAChT expression also increases the frequency of release, presumably by increasing the detection of events, but increased VAChT expression may also increase the number of SVs capable of transmitter release. Neutralization of an aspartate in TMD10 of VAChT reduces the amount of transmitter packaged by the endogeneous wild-type transporter, possibly by promoting efflux.
    • Song H-j, Ming G-I, Fon E, Bellocchio E, Edwards RH, Poo M-m. Expression of putative vesicular acetylcholine transporter facilitates quantal transmitter packaging. of outstanding interest Neuron. 18:1997;815-826 Using a Xenopus culture system in which motor neurons form synapses with muscle cells, expression of VAChT in the motor neurons but not the muscle cells increases quantal size, indicating that the transporter can limit the rate of SV filling. VAChT expression also increases the frequency of release, presumably by increasing the detection of events, but increased VAChT expression may also increase the number of SVs capable of transmitter release. Neutralization of an aspartate in TMD10 of VAChT reduces the amount of transmitter packaged by the endogeneous wild-type transporter, possibly by promoting efflux.
    • (1997) Neuron , vol.18 , pp. 815-826
    • Song H-J1    Ming G-I2    Fon, E.3    Bellocchio, E.4    Edwards, R.H.5    Poo M-M6
  • 17
    • 0028263975 scopus 로고
    • The chromaffin granule and synaptic vesicle amine transporters differ in substrate recognition and sensitivity to inhibitors
    • Peter D, Jimenez J, Liu Y, Kim J, Edwards RH. The chromaffin granule and synaptic vesicle amine transporters differ in substrate recognition and sensitivity to inhibitors. J Biol Chem. 269:1994;7231-7237.
    • (1994) J Biol Chem , vol.269 , pp. 7231-7237
    • Peter, D.1    Jimenez, J.2    Liu, Y.3    Kim, J.4    Edwards, R.H.5
  • 18
    • 0023688990 scopus 로고
    • Cholinergic synaptic vesicle heterogeneity: Evidence for regulation of acetylcholine transport
    • Gracz LM, Wang W-C, Parsons SM. Cholinergic synaptic vesicle heterogeneity: evidence for regulation of acetylcholine transport. Biochemistry. 27:1988;5268-5274.
    • (1988) Biochemistry , vol.27 , pp. 5268-5274
    • Gracz, L.M.1    Wang W-C2    Parsons, S.M.3
  • 19
    • 0030931721 scopus 로고    scopus 로고
    • VMAT2 knockout mice: Heterozygous display reduced amphetamine-conditioned reward, enhanced amphetamine locomotion and enhanced MPTP toxicity
    • +/- mice show slightly increased sensitivity to the neurotoxin MPTP, consistent with a role for VMAT2 in protection against this form of toxicity (see Liu et al., 1992 [8]).
    • +/- mice show slightly increased sensitivity to the neurotoxin MPTP, consistent with a role for VMAT2 in protection against this form of toxicity (see Liu et al., 1992 [8]).
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9938-9943
    • Takahashi, N.1    Miner, L.L.2    Sora, I.3    Ujike, H.4    Revay, R.S.5    Kostic, V.6    Jackson-Lewis, V.7    Przedborski, S.8    Uhl, G.R.9
  • 20
    • 0031458637 scopus 로고    scopus 로고
    • Vesicular transport regulates monoamine storage and release but is not essential for amphetamine action
    • -/- animals and permits survival to several weeks. Heterozygotes show substantially reduced brain monoamine levels, presumably accounting for the behavioral defects observed in Takahashi et al., 1997 [19] and Wang et al., 1997 [21] and supporting a role for the vesicular transporters in regulating transmitter release.
    • -/- animals and permits survival to several weeks. Heterozygotes show substantially reduced brain monoamine levels, presumably accounting for the behavioral defects observed in Takahashi et al., 1997 [19] and Wang et al., 1997 [21] and supporting a role for the vesicular transporters in regulating transmitter release.
    • (1997) Neuron , vol.19 , pp. 1271-1283
    • Fon, E.A.1    Pothos, E.N.2    Sun B-C3    Killeen, N.4    Sulzer, D.5    Edwards, R.H.6
  • 22
    • 0025122167 scopus 로고
    • Induction of the vesicular monoamine transporter by elevated potassium concentration in culture of rat sympathetic neurons
    • Desnos C, Raynaud B, Vidal S, Weber MJ, Scherman D. Induction of the vesicular monoamine transporter by elevated potassium concentration in culture of rat sympathetic neurons. Dev Brain Res. 52:1990;161-166.
    • (1990) Dev Brain Res , vol.52 , pp. 161-166
    • Desnos, C.1    Raynaud, B.2    Vidal, S.3    Weber, M.J.4    Scherman, D.5
  • 23
    • 0026523851 scopus 로고
    • Regulation of the chromaffin granule catecholamine transporter in cultured bovine adrenal medullary cell-stimulus biosynthesis coupling
    • Desnos C, Laran M, Scherman D. Regulation of the chromaffin granule catecholamine transporter in cultured bovine adrenal medullary cell-stimulus biosynthesis coupling. J Neurochem. 59:1992;2105-2112.
    • (1992) J Neurochem , vol.59 , pp. 2105-2112
    • Desnos, C.1    Laran, M.2    Scherman, D.3
  • 25
    • 0025908023 scopus 로고
    • ATP-dependent uptake of 5-hydroxytryptamine by secretory granules isolated from thyroid parafollicular cells
    • Cidon S, Tamir H, Nunez EA, Gershon MD. ATP-dependent uptake of 5-hydroxytryptamine by secretory granules isolated from thyroid parafollicular cells. J Biol Chem. 266:1991;4392-4400.
    • (1991) J Biol Chem , vol.266 , pp. 4392-4400
    • Cidon, S.1    Tamir, H.2    Nunez, E.A.3    Gershon, M.D.4
  • 27
    • 0029147857 scopus 로고
    • Effects of protein kinase inhibitors and protein phosphatase inhibitors on cyclic AMP-dependent down-regulation of vesicular monoamine transport in pheochromocytoma PC12 cells
    • Nakanishi N, Onozawa S, Matsumoto R, Hasegawa H, Yamada S. Effects of protein kinase inhibitors and protein phosphatase inhibitors on cyclic AMP-dependent down-regulation of vesicular monoamine transport in pheochromocytoma PC12 cells. FEBS Lett. 368:1995;411-414.
    • (1995) FEBS Lett , vol.368 , pp. 411-414
    • Nakanishi, N.1    Onozawa, S.2    Matsumoto, R.3    Hasegawa, H.4    Yamada, S.5
  • 28
    • 0030965452 scopus 로고    scopus 로고
    • Phosphorylation of a vesicular monoamine transporter by casein kinase II
    • Krantz DE, Peter D, Liu Y, Edwards RH. Phosphorylation of a vesicular monoamine transporter by casein kinase II. J Biol Chem. 272:1997;6752-6759.
    • (1997) J Biol Chem , vol.272 , pp. 6752-6759
    • Krantz, D.E.1    Peter, D.2    Liu, Y.3    Edwards, R.H.4
  • 29
    • 0027392598 scopus 로고
    • Time course of extracellular dopamine and behavioral sensitization to cocaine. II. Dopamine perikarya
    • Kalivas PW, Duffy P. Time course of extracellular dopamine and behavioral sensitization to cocaine. II. Dopamine perikarya. J Neurosci. 13:1993;276-284.
    • (1993) J Neurosci , vol.13 , pp. 276-284
    • Kalivas, P.W.1    Duffy, P.2
  • 30
    • 0029071155 scopus 로고
    • The vesicular monoamine transporter-2 is present in small synaptic vesicles and preferentially localizes to large dense core vesicles in rat solitary tract nuclei
    • Nirenberg MJ, Liu Y, Peter D, Edwards RH, Pickel VM. The vesicular monoamine transporter-2 is present in small synaptic vesicles and preferentially localizes to large dense core vesicles in rat solitary tract nuclei. Proc Natl Acad Sci USA. 92:1995;8773-8777.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8773-8777
    • Nirenberg, M.J.1    Liu, Y.2    Peter, D.3    Edwards, R.H.4    Pickel, V.M.5
  • 31
    • 0029898811 scopus 로고    scopus 로고
    • Ultrastructural localization of the vesicular monoamine transporter-2 in midbrain dopaminergic neurons: Potential sites for somatodendritic storage and release of dopamine
    • of special interest. VMAT2 occurs in tubulovesicular structures of midbrain dopamine cell bodies and dendrites as well as in SVs and LDCVs in striatal terminals. Although these structures may simply represent an intermediate in transit from one compartment to another, these vesicles may also mediate the release of dopamine from midbrain cell bodies and dendrites described in Kalivas and Duffy, 1993 [29].
    • Nirenberg MJ, Chan J, Liu Y, Edwards RH, Pickel VM. Ultrastructural localization of the vesicular monoamine transporter-2 in midbrain dopaminergic neurons: potential sites for somatodendritic storage and release of dopamine. of special interest J Neurosci. 16:1996;4135-4145 VMAT2 occurs in tubulovesicular structures of midbrain dopamine cell bodies and dendrites as well as in SVs and LDCVs in striatal terminals. Although these structures may simply represent an intermediate in transit from one compartment to another, these vesicles may also mediate the release of dopamine from midbrain cell bodies and dendrites described in Kalivas and Duffy, 1993 [29].
    • (1996) J Neurosci , vol.16 , pp. 4135-4145
    • Nirenberg, M.J.1    Chan, J.2    Liu, Y.3    Edwards, R.H.4    Pickel, V.M.5
  • 32
    • 0027971587 scopus 로고
    • Preferential localization of a vesicular monoamine transporter to dense core vesicles in PC12 cells
    • Liu Y, Schweitzer ES, Nirenberg MJ, Pickel VM, Evans CJ, Edwards RH. Preferential localization of a vesicular monoamine transporter to dense core vesicles in PC12 cells. J Cell Biol. 127:1994;1419-1433.
    • (1994) J Cell Biol , vol.127 , pp. 1419-1433
    • Liu, Y.1    Schweitzer, E.S.2    Nirenberg, M.J.3    Pickel, V.M.4    Evans, C.J.5    Edwards, R.H.6
  • 33
    • 0027179911 scopus 로고
    • Selective storge of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin
    • Bauerfeind R, Regnier-Vigouroux A, Flatmark T, Huttner WB. Selective storge of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin. Neuron. 11:1993;105-121.
    • (1993) Neuron , vol.11 , pp. 105-121
    • Bauerfeind, R.1    Regnier-Vigouroux, A.2    Flatmark, T.3    Huttner, W.B.4
  • 34
    • 0029939094 scopus 로고    scopus 로고
    • Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles
    • of special interest. Immuno-electron microscopy demonstrates VAChT in SVs of rat brain and in SLMVs of PC12 cells, supporting the difference in localization from that of the VMATs.
    • Weihe E, Tao-Cheng J-H, Schafer MK-H, Erickson JD, Eiden LE. Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles. of special interest Proc Natl Acad Sci USA. 93:1996;3547-3552 Immuno-electron microscopy demonstrates VAChT in SVs of rat brain and in SLMVs of PC12 cells, supporting the difference in localization from that of the VMATs.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3547-3552
    • Weihe, E.1    Tao-Cheng J-H2    Schafer Mk-H3    Erickson, J.D.4    Eiden, L.E.5
  • 35
    • 0028845359 scopus 로고
    • Identification of residues involved in substrate recognition by a vesicular monoamine transporter
    • Merickel A, Rosandich P, Peter D, Edwards RH. Identification of residues involved in substrate recognition by a vesicular monoamine transporter. J Biol Chem. 270:1995;25798-25804.
    • (1995) J Biol Chem , vol.270 , pp. 25798-25804
    • Merickel, A.1    Rosandich, P.2    Peter, D.3    Edwards, R.H.4
  • 36
    • 0031054527 scopus 로고    scopus 로고
    • Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrates recognition
    • of special interest. of special interest. A highly conserved lysine in TMD2 of VMAT2 forms a charge pair with a highly conserved aspartate in TMD11. Neutralization of each residues alone eliminates transport activity but neutralization of both restores function, providing some of the first information about the packing of helices in these proteins.
    • of special interest Merickel A, Kaback HR, Edwards RH. Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrates recognition. of special interest J Biol Chem. 272:1997;5403-5408 A highly conserved lysine in TMD2 of VMAT2 forms a charge pair with a highly conserved aspartate in TMD11. Neutralization of each residues alone eliminates transport activity but neutralization of both restores function, providing some of the first information about the packing of helices in these proteins.
    • (1997) J Biol Chem , vol.272 , pp. 5403-5408
    • Merickel, A.1    Kaback, H.R.2    Edwards, R.H.3
  • 37
    • 17544366949 scopus 로고    scopus 로고
    • Modification of the pH profile and tetrabenazine sensitivity of rat VMAT1 by replacement of aspartate 404 with glutamate
    • + as measured by reserpine binding. Supporting a role for this residue in proton translocation, replacement of the aspartate with glutamate alters the pH profile for transport.
    • + as measured by reserpine binding. Supporting a role for this residue in proton translocation, replacement of the aspartate with glutamate alters the pH profile for transport.
    • (1996) J Biol Chem , vol.271 , pp. 13048-13054
    • Steiner-Mordoch, S.1    Shirvan, A.2    Schuldiner, S.3
  • 38
    • 0027272707 scopus 로고
    • Genes required for GABA function in Caenorhabditis elegans
    • McIntire S, Jorgensen E, Horvitz HR. Genes required for GABA function in Caenorhabditis elegans. Nature. 364:1993;337-341.
    • (1993) Nature , vol.364 , pp. 337-341
    • McIntire, S.1    Jorgensen, E.2    Horvitz, H.R.3
  • 39
    • 0030734546 scopus 로고    scopus 로고
    • Identification and characterization of the vesicular GABA transporter
    • of special interest. This report describes the identification of a genomic fragment from C. elegans that complements the defect in unc-47, a mutant with a presynaptic defect in GABAergic transmission. A vertebrate homolog has a pattern of expression restricted to GABAergic cell groups and, further, confers vesicular GABA transport with the expected properties on heterologous expression. The sequence predicts 10 TMDs and a relatively large cytoplasmic amino terminus.In addition, it defines a novel family of vesicular neurotransmitter transports that may also include a transporter for the principal excitatory neurotransmitter, glutamate.
    • McIntire SL, Reimer RJ, Schuske K, Edwards RH, Jorgensen EM. Identification and characterization of the vesicular GABA transporter. of special interest Nature. 389:1997;870-876 This report describes the identification of a genomic fragment from C. elegans that complements the defect in unc-47, a mutant with a presynaptic defect in GABAergic transmission. A vertebrate homolog has a pattern of expression restricted to GABAergic cell groups and, further, confers vesicular GABA transport with the expected properties on heterologous expression. The sequence predicts 10 TMDs and a relatively large cytoplasmic amino terminus.In addition, it defines a novel family of vesicular neurotransmitter transports that may also include a transporter for the principal excitatory neurotransmitter, glutamate.
    • (1997) Nature , vol.389 , pp. 870-876
    • McIntire, S.L.1    Reimer, R.J.2    Schuske, K.3    Edwards, R.H.4    Jorgensen, E.M.5
  • 40
    • 0008224051 scopus 로고
    • Active transport of gamma-aminobutyric acid and glycine into synaptic vesicles
    • Kish PE, Fischer-Bovenkerk C, Ueda T. Active transport of gamma-aminobutyric acid and glycine into synaptic vesicles. Proc Natl Acad Sci USA. 86:1989;3877-3881.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3877-3881
    • Kish, P.E.1    Fischer-Bovenkerk, C.2    Ueda, T.3
  • 41
    • 0025813176 scopus 로고
    • GABA and glycine in synaptic vesicles: Storage and transport characteristics
    • Burger PM, Hell J, Mehl E, Krasel C, Lottspeich F, Jahn R. GABA and glycine in synaptic vesicles: storage and transport characteristics. Neuron. 7:1991;287-293.
    • (1991) Neuron , vol.7 , pp. 287-293
    • Burger, P.M.1    Hell, J.2    Mehl, E.3    Krasel, C.4    Lottspeich, F.5    Jahn, R.6
  • 42
    • 0030840107 scopus 로고    scopus 로고
    • Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases
    • Sagne C, El Mestikawy S, Isambert M-F, Hamon M, Henry J-P, Giros B, Gasnier B. Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases. FEBS Lett. 417:1997;177-183.
    • (1997) FEBS Lett , vol.417 , pp. 177-183
    • Sagne, C.1    El Mestikawy, S.2    Isambert M-F3    Hamon, M.4    Henry J-P5    Giros, B.6    Gasnier, B.7
  • 43
    • 0030891312 scopus 로고    scopus 로고
    • A protein factor that inhibits ATP-dependent glutamate and γ-aminobutyric acid accumulation into synaptic vesicles: Purification and initial characterization
    • of special interest. Using native synaptic vesicles to assay vesicular glutamate and GABA transport, an inhibitory protein was identified as a proteolytic fragment of fodrin, suggesting a novel interaction between synaptic vesicles and the cytoskeleton.
    • Ozkan ED, Lee FS, Ueda T. A protein factor that inhibits ATP-dependent glutamate and γ-aminobutyric acid accumulation into synaptic vesicles: purification and initial characterization. of special interest Proc Natl Acad Sci USA. 94:1997;4137-4142 Using native synaptic vesicles to assay vesicular glutamate and GABA transport, an inhibitory protein was identified as a proteolytic fragment of fodrin, suggesting a novel interaction between synaptic vesicles and the cytoskeleton.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4137-4142
    • Ozkan, E.D.1    Lee, F.S.2    Ueda, T.3
  • 44
    • 0029007621 scopus 로고
    • Substrate specificity and expression profile of amino acid transporters (AAPs) in Arabidopsis
    • Fischer WN, Kwart M, Hummel S, Frommer WB. Substrate specificity and expression profile of amino acid transporters (AAPs) in Arabidopsis. J Biol Chem. 270:1995;16315-16320.
    • (1995) J Biol Chem , vol.270 , pp. 16315-16320
    • Fischer, W.N.1    Kwart, M.2    Hummel, S.3    Frommer, W.B.4


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