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Article ; Online: The structure of NAD

2023 Volume 299, Issue 11, Page(s) 105290

Abstract: Toll-like and interleukin-1/18 receptor/resistance (TIR) domain-containing proteins function as important signaling and immune regulatory molecules. TIR domain-containing proteins identified in eukaryotic and prokaryotic species also exhibit NAD+ ... ...

Abstract	Toll-like and interleukin-1/18 receptor/resistance (TIR) domain-containing proteins function as important signaling and immune regulatory molecules. TIR domain-containing proteins identified in eukaryotic and prokaryotic species also exhibit NAD+ hydrolase activity in select bacteria, plants, and mammalian cells. We report the crystal structure of the Acinetobacter baumannii TIR domain protein (AbTir-TIR) with confirmed NAD
MeSH term(s)	Acinetobacter baumannii/genetics ; Acinetobacter baumannii/metabolism ; Bacteria/metabolism ; Bacterial Proteins/metabolism ; Deuterium ; Hydrolases/metabolism ; Mammals/metabolism ; NAD/metabolism ; Protein Domains
Chemical Substances	Bacterial Proteins ; Deuterium (AR09D82C7G) ; Hydrolases (EC 3.-) ; NAD (0U46U6E8UK)
Language	English
Publishing date	2023-09-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105290
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Article ; Online: Natural antisense transcripts regulate the neuronal stress response and excitability.

Zheng, Xingguo / Valakh, Vera / Diantonio, Aaron / Ben-Shahar, Yehuda

eLife

2014 Volume 3, Page(s) e01849

Abstract: Neurons regulate ionic fluxes across their plasma membrane to maintain their excitable properties under varying environmental conditions. However, the mechanisms that regulate ion channels abundance remain poorly understood. Here we show that pickpocket ... ...

Abstract	Neurons regulate ionic fluxes across their plasma membrane to maintain their excitable properties under varying environmental conditions. However, the mechanisms that regulate ion channels abundance remain poorly understood. Here we show that pickpocket 29 (ppk29), a gene that encodes a Drosophila degenerin/epithelial sodium channel (DEG/ENaC), regulates neuronal excitability via a protein-independent mechanism. We demonstrate that the mRNA 3'UTR of ppk29 affects neuronal firing rates and associated heat-induced seizures by acting as a natural antisense transcript (NAT) that regulates the neuronal mRNA levels of seizure (sei), the Drosophila homolog of the human Ether-à-go-go Related Gene (hERG) potassium channel. We find that the regulatory impact of ppk29 mRNA on sei is independent of the sodium channel it encodes. Thus, our studies reveal a novel mRNA dependent mechanism for the regulation of neuronal excitability that is independent of protein-coding capacity. DOI: http://dx.doi.org/10.7554/eLife.01849.001.
MeSH term(s)	3' Untranslated Regions ; Action Potentials ; Animals ; Animals, Genetically Modified ; Behavior, Animal ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Ether-A-Go-Go Potassium Channels/genetics ; Ether-A-Go-Go Potassium Channels/metabolism ; Gene Expression Regulation ; Genotype ; Heat-Shock Response ; Ion Channels/genetics ; Ion Channels/metabolism ; Locomotion ; Mutation ; Neurons/metabolism ; Phenotype ; RNA Interference ; RNA, Antisense/genetics ; RNA, Antisense/metabolism ; RNA, Messenger/metabolism ; RNA, Small Interfering/metabolism ; Time Factors ; Transcription, Genetic
Chemical Substances	3' Untranslated Regions ; Drosophila Proteins ; Ether-A-Go-Go Potassium Channels ; Ion Channels ; PPK29 protein, Drosophila ; RNA, Antisense ; RNA, Messenger ; RNA, Small Interfering ; eag protein, Drosophila
Language	English
Publishing date	2014-01-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.01849
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Article ; Online: Rab3-GEF Controls Active Zone Development at the Drosophila Neuromuscular Junction.

Bae, Haneui / Chen, Shirui / Roche, John P / Ai, Minrong / Wu, Chunlai / Diantonio, Aaron / Graf, Ethan R

eNeuro

2016 Volume 3, Issue 2

Abstract: Synaptic signaling involves the release of neurotransmitter from presynaptic active zones (AZs). Proteins that regulate vesicle exocytosis cluster at AZs, composing the cytomatrix at the active zone (CAZ). At the Drosophila neuromuscular junction (NMJ), ... ...

Abstract	Synaptic signaling involves the release of neurotransmitter from presynaptic active zones (AZs). Proteins that regulate vesicle exocytosis cluster at AZs, composing the cytomatrix at the active zone (CAZ). At the Drosophila neuromuscular junction (NMJ), the small GTPase Rab3 controls the distribution of CAZ proteins across release sites, thereby regulating the efficacy of individual AZs. Here we identify Rab3-GEF as a second protein that acts in conjunction with Rab3 to control AZ protein composition. At rab3-GEF mutant NMJs, Bruchpilot (Brp) and Ca(2+) channels are enriched at a subset of AZs, leaving the remaining sites devoid of key CAZ components in a manner that is indistinguishable from rab3 mutant NMJs. As the Drosophila homologue of mammalian DENN/MADD and Caenorhabditis elegans AEX-3, Rab3-GEF is a guanine nucleotide exchange factor (GEF) for Rab3 that stimulates GDP to GTP exchange. Mechanistic studies reveal that although Rab3 and Rab3-GEF act within the same mechanism to control AZ development, Rab3-GEF is involved in multiple roles. We show that Rab3-GEF is required for transport of Rab3. However, the synaptic phenotype in the rab3-GEF mutant cannot be fully explained by defective transport and loss of GEF activity. A transgenically expressed GTP-locked variant of Rab3 accumulates at the NMJ at wild-type levels and fully rescues the rab3 mutant but is unable to rescue the rab3-GEF mutant. Our results suggest that although Rab3-GEF acts upstream of Rab3 to control Rab3 localization and likely GTP-binding, it also acts downstream to regulate CAZ development, potentially as a Rab3 effector at the synapse.
MeSH term(s)	Action Potentials/genetics ; Analysis of Variance ; Animals ; Animals, Genetically Modified ; Drosophila ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Gene Expression Regulation, Developmental/genetics ; Microscopy, Confocal ; Mutation/genetics ; Neuromuscular Junction/cytology ; Neuromuscular Junction/genetics ; Neurons/physiology ; Patch-Clamp Techniques ; Presynaptic Terminals/physiology ; rab3 GTP-Binding Proteins/genetics ; rab3 GTP-Binding Proteins/metabolism
Chemical Substances	BRP protein, Drosophila ; Drosophila Proteins ; rab3 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2016-03-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2800598-3
ISSN	2373-2822 ; 2373-2822
ISSN (online)	2373-2822
ISSN	2373-2822
DOI	10.1523/ENEURO.0031-16.2016
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Article ; Online: A tyrosine-based motif localizes a Drosophila vesicular transporter to synaptic vesicles in vivo.

Grygoruk, Anna / Fei, Hao / Daniels, Richard W / Miller, Bradley R / Diantonio, Aaron / Krantz, David E

The Journal of biological chemistry

2010 Volume 285, Issue 10, Page(s) 6867–6878

Abstract: Vesicular neurotransmitter transporters must localize to synaptic vesicles (SVs) to allow regulated neurotransmitter release at the synapse. However, the signals required to localize vesicular proteins to SVs in vivo remain unclear. To address this ... ...

Abstract	Vesicular neurotransmitter transporters must localize to synaptic vesicles (SVs) to allow regulated neurotransmitter release at the synapse. However, the signals required to localize vesicular proteins to SVs in vivo remain unclear. To address this question we have tested the effects of mutating proposed trafficking domains in Drosophila orthologs of the vesicular monoamine and glutamate transporters, DVMAT-A and DVGLUT. We show that a tyrosine-based motif (YXXY) is important both for DVMAT-A internalization from the cell surface in vitro, and localization to SVs in vivo. In contrast, DVGLUT deletion mutants that lack a putative C-terminal trafficking domain show more modest defects in both internalization in vitro and trafficking to SVs in vivo. Our data show for the first time that mutation of a specific trafficking motif can disrupt localization to SVs in vivo and suggest possible differences in the sorting of VMATs versus VGLUTs to SVs at the synapse.
MeSH term(s)	Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Endocytosis/physiology ; Humans ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Sequence Alignment ; Synaptic Transmission/physiology ; Synaptic Vesicles/metabolism ; Tyrosine/metabolism ; Vesicular Glutamate Transport Proteins/genetics ; Vesicular Glutamate Transport Proteins/metabolism ; Vesicular Monoamine Transport Proteins/genetics ; Vesicular Monoamine Transport Proteins/metabolism
Chemical Substances	Drosophila Proteins ; Vesicular Glutamate Transport Proteins ; Vesicular Monoamine Transport Proteins ; Tyrosine (42HK56048U)
Language	English
Publishing date	2010-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.M109.073064
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Article ; Online: Protein turnover of the Wallenda/DLK kinase regulates a retrograde response to axonal injury.

Xiong, Xin / Wang, Xin / Ewanek, Ronny / Bhat, Pavan / Diantonio, Aaron / Collins, Catherine A

The Journal of cell biology

2010 Volume 191, Issue 1, Page(s) 211–223

Abstract: Regenerative responses to axonal injury involve changes in gene expression; however, little is known about how such changes can be induced from a distant site of injury. In this study, we describe a nerve crush assay in Drosophila melanogaster to study ... ...

Abstract	Regenerative responses to axonal injury involve changes in gene expression; however, little is known about how such changes can be induced from a distant site of injury. In this study, we describe a nerve crush assay in Drosophila melanogaster to study injury signaling and regeneration mechanisms. We find that Wallenda (Wnd), a conserved mitogen-activated protein kinase (MAPK) kinase kinase homologous to dual leucine zipper kinase, functions as an upstream mediator of a cell-autonomous injury signaling cascade that involves the c-Jun NH(2)-terminal kinase MAPK and Fos transcription factor. Wnd is physically transported in axons, and axonal transport is required for the injury signaling mechanism. Wnd is regulated by a conserved E3 ubiquitin ligase, named Highwire (Hiw) in Drosophila. Injury induces a rapid increase in Wnd protein concomitantly with a decrease in Hiw protein. In hiw mutants, injury signaling is constitutively active, and neurons initiate a faster regenerative response. Our data suggest that the regulation of Wnd protein turnover by Hiw can function as a damage surveillance mechanism for responding to axonal injury.
MeSH term(s)	Animals ; Axons/physiology ; Cell Nucleus/metabolism ; Cell Nucleus/ultrastructure ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila Proteins/physiology ; Drosophila melanogaster/cytology ; Drosophila melanogaster/enzymology ; Drosophila melanogaster/physiology ; Gene Expression Regulation ; MAP Kinase Kinase Kinases/genetics ; MAP Kinase Kinase Kinases/metabolism ; MAP Kinase Kinase Kinases/physiology ; Mutation ; Nerve Regeneration ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/physiology ; Neurons/cytology ; Neurons/metabolism ; Neurons/physiology ; Phosphoprotein Phosphatases/metabolism ; Protein Transport ; Proto-Oncogene Proteins c-jun/metabolism ; Proto-Oncogene Proteins c-jun/physiology ; Signal Transduction
Chemical Substances	Drosophila Proteins ; HIW protein, Drosophila ; Nerve Tissue Proteins ; Proto-Oncogene Proteins c-jun ; kay protein, Drosophila ; MAP Kinase Kinase Kinases (EC 2.7.11.25) ; wnd protein, Drosophila (EC 2.7.11.25) ; puc protein, Drosophila (EC 3.1.3.-) ; Phosphoprotein Phosphatases (EC 3.1.3.16)
Language	English
Publishing date	2010-10-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201006039
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Article ; Online: Unc-51 controls active zone density and protein composition by downregulating ERK signaling.

Wairkar, Yogesh P / Toda, Hirofumi / Mochizuki, Hiroaki / Furukubo-Tokunaga, Katsuo / Tomoda, Toshifumi / Diantonio, Aaron

The Journal of neuroscience : the official journal of the Society for Neuroscience

2009 Volume 29, Issue 2, Page(s) 517–528

Abstract: Efficient synaptic transmission requires the apposition of neurotransmitter release sites opposite clusters of postsynaptic neurotransmitter receptors. Transmitter is released at active zones, which are composed of a large complex of proteins necessary ... ...

Abstract	Efficient synaptic transmission requires the apposition of neurotransmitter release sites opposite clusters of postsynaptic neurotransmitter receptors. Transmitter is released at active zones, which are composed of a large complex of proteins necessary for synaptic development and function. Many active zone proteins have been identified, but little is known of the mechanisms that ensure that each active zone receives the proper complement of proteins. Here we use a genetic analysis in Drosophila to demonstrate that the serine threonine kinase Unc-51 acts in the presynaptic motoneuron to regulate the localization of the active zone protein Bruchpilot opposite to glutamate receptors at each synapse. In the absence of Unc-51, many glutamate receptor clusters are unapposed to Bruchpilot, and ultrastructural analysis demonstrates that fewer active zones contain dense body T-bars. In addition to the presence of these aberrant synapses, there is also a decrease in the density of all synapses. This decrease in synaptic density and abnormal active zone composition is associated with impaired evoked transmitter release. Mechanistically, Unc-51 inhibits the activity of the MAP kinase ERK to promote synaptic development. In the unc-51 mutant, increased ERK activity leads to the decrease in synaptic density and the absence of Bruchpilot from many synapses. Hence, activated ERK negatively regulates synapse formation, resulting in either the absence of active zones or the formation of active zones without their proper complement of proteins. The Unc-51-dependent inhibition of ERK activity provides a potential mechanism for synapse-specific control of active zone protein composition and release probability.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Axonal Transport/genetics ; Down-Regulation/genetics ; Down-Regulation/physiology ; Drosophila ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Extracellular Signal-Regulated MAP Kinases/genetics ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Microscopy, Electron, Transmission ; Miniature Postsynaptic Potentials ; Mutation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/physiology ; Receptors, Glutamate/genetics ; Receptors, Glutamate/metabolism ; Signal Transduction/genetics ; Signal Transduction/physiology ; Synapses/physiology ; Synapses/ultrastructure
Chemical Substances	BRP protein, Drosophila ; Drosophila Proteins ; Receptors, Glutamate ; glutamate receptor III, Drosophila ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2009-01-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.3848-08.2009
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Article: Control of a kinesin-cargo linkage mechanism by JNK pathway kinases.

Horiuchi, Dai / Collins, Catherine A / Bhat, Pavan / Barkus, Rosemarie V / Diantonio, Aaron / Saxton, William M

Current biology : CB

2007 Volume 17, Issue 15, Page(s) 1313–1317

Abstract: Long-distance organelle transport toward axon terminals, critical for neuron development and function, is driven along microtubules by kinesins [1, 2]. The biophysics of force production by various kinesins is known in detail. However, the mechanisms of ... ...

Abstract	Long-distance organelle transport toward axon terminals, critical for neuron development and function, is driven along microtubules by kinesins [1, 2]. The biophysics of force production by various kinesins is known in detail. However, the mechanisms of in vivo transport processes are poorly understood because little is known about how motor-cargo linkages are controlled. A c-Jun N-terminal kinase (JNK)-interacting protein (JIP1) has been identified previously as a linker between kinesin-1 and certain vesicle membrane proteins, such as Alzheimer's APP protein and a reelin receptor ApoER2 [3, 4]. JIPs are also known to be scaffolding proteins for JNK pathway kinases [5, 6]. Here, we report evidence that a Drosophila ubiquitin-specific hydrolase and a JNK signaling pathway that it modulates can regulate a JIP1-kinesin linkage. The JNK pathway includes a MAPKKK (Wallenda/DLK), a MAPKK (Hemipterous/MKK7), and the Drosophila JNK homolog Basket. Genetic tests indicate that those kinases are required for normal axonal transport. Biochemical tests show that activation of Wallenda (DLK) and Hemipterous (MKK7) disrupts binding between kinesin-1 and APLIP1, which is the Drosophila JIP1 homolog. This suggests a control mechanism in which an activated JNK pathway influences axonal transport by functioning as a kinesin-cargo dissociation factor.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Axonal Transport ; Biological Transport ; Carrier Proteins/metabolism ; Drosophila/metabolism ; Drosophila Proteins/metabolism ; JNK Mitogen-Activated Protein Kinases/metabolism ; Kinesin/metabolism ; Microtubules/metabolism
Chemical Substances	APP-like protein interacting protein 1, Drosophila ; Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Drosophila Proteins ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2007-08-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2007.06.062
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Article: Drosophila vesicular monoamine transporter mutants can adapt to reduced or eliminated vesicular stores of dopamine and serotonin.

Simon, Anne F / Daniels, Richard / Romero-Calderón, Rafael / Grygoruk, Anna / Chang, Hui-Yun / Najibi, Rod / Shamouelian, David / Salazar, Evelyn / Solomon, Mordecai / Ackerson, Larry C / Maidment, Nigel T / Diantonio, Aaron / Krantz, David E

Genetics

2008 Volume 181, Issue 2, Page(s) 525–541

Abstract: Physiologic and pathogenic changes in amine release induce dramatic behavioral changes, but the underlying cellular mechanisms remain unclear. To investigate these adaptive processes, we have characterized mutations in the Drosophila vesicular monoamine ... ...

Abstract	Physiologic and pathogenic changes in amine release induce dramatic behavioral changes, but the underlying cellular mechanisms remain unclear. To investigate these adaptive processes, we have characterized mutations in the Drosophila vesicular monoamine transporter (dVMAT), which is required for the vesicular storage of dopamine, serotonin, and octopamine. dVMAT mutant larvae show reduced locomotion and decreased electrical activity in motoneurons innervating the neuromuscular junction (NMJ) implicating central amines in the regulation of these activities. A parallel increase in evoked glutamate release by the motoneuron is consistent with a homeostatic adaptation at the NMJ. Despite the importance of aminergic signaling for regulating locomotion and other behaviors, adult dVMAT homozygous null mutants survive under conditions of low population density, thus allowing a phenotypic characterization of adult behavior. Homozygous mutant females are sterile and show defects in both egg retention and development; males also show reduced fertility. Homozygotes show an increased attraction to light but are mildly impaired in geotaxis and escape behaviors. In contrast, heterozygous mutants show an exaggerated escape response. Both hetero- and homozygous mutants demonstrate an altered behavioral response to cocaine. dVMAT mutants define potentially adaptive responses to reduced or eliminated aminergic signaling and will be useful to identify the underlying molecular mechanisms.
MeSH term(s)	Animals ; Behavior, Animal/drug effects ; Cocaine/pharmacology ; Dopamine/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/drug effects ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Female ; Genes, Insect ; Infertility/genetics ; Infertility/metabolism ; Male ; Mutation ; Neuromuscular Junction/metabolism ; Octopamine/metabolism ; Oogenesis/genetics ; Phenotype ; Photobiology ; Serotonin/metabolism ; Vesicular Monoamine Transport Proteins/genetics ; Vesicular Monoamine Transport Proteins/metabolism
Chemical Substances	Drosophila Proteins ; Vesicular Monoamine Transport Proteins ; Octopamine (14O50WS8JD) ; Serotonin (333DO1RDJY) ; Cocaine (I5Y540LHVR) ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2008-11-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1534/genetics.108.094110
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Article: A splice variant of the Drosophila vesicular monoamine transporter contains a conserved trafficking domain and functions in the storage of dopamine, serotonin, and octopamine.

Greer, Christina L / Grygoruk, Anna / Patton, David E / Ley, Brett / Romero-Calderon, Rafael / Chang, Hui-Yun / Houshyar, Roozbeh / Bainton, Roland J / Diantonio, Aaron / Krantz, David E

Journal of neurobiology

2005 Volume 64, Issue 3, Page(s) 239–258

Abstract: Vesicular monoamine transporters (VMATs) mediate the transport of dopamine (DA), serotonin (5HT), and other monoamines into secretory vesicles. The regulation of mammalian VMAT and the related vesicular acetylcholine transporter (VAChT) has been proposed ...

Abstract	Vesicular monoamine transporters (VMATs) mediate the transport of dopamine (DA), serotonin (5HT), and other monoamines into secretory vesicles. The regulation of mammalian VMAT and the related vesicular acetylcholine transporter (VAChT) has been proposed to involve membrane trafficking, but the mechanisms remain unclear. To facilitate a genetic analysis of vesicular transporter function and regulation, we have cloned the Drosophila homolog of the vesicular monoamine transporter (dVMAT). We identify two mRNA splice variants (DVMAT-A and B) that differ at their C-terminus, the domain responsible for endocytosis of mammalian VMAT and VAChT. DVMAT-A contains trafficking motifs conserved in mammals but not C. elegans, and internalization assays indicate that the DVMAT-A C-terminus is involved in endocytosis. DVMAT-B contains a divergent C-terminal domain and is less efficiently internalized from the cell surface. Using in vitro transport assays, we show that DVMAT-A recognizes DA, 5HT, octopamine, tyramine, and histamine as substrates, and similar to mammalian VMAT homologs, is inhibited by the drug reserpine and the environmental toxins 2,2,4,5,6-pentachlorobiphenyl and heptachlor. We have developed a specific antiserum to DVMAT-A, and find that it localizes to dopaminergic and serotonergic neurons as well as octopaminergic, type II terminals at the neuromuscular junction. Surprisingly, DVMAT-A is co-expressed at type II terminals with the Drosophila vesicular glutamate transporter. Our data suggest that DVMAT-A functions as a vesicular transporter for DA, 5HT, and octopamine in vivo, and will provide a powerful invertebrate model for the study of transporter trafficking and regulation.
MeSH term(s)	Adrenergic Uptake Inhibitors/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; COS Cells ; Cercopithecus aethiops ; Dopamine/metabolism ; Drosophila ; Endocytosis/drug effects ; Endocytosis/physiology ; Fluorescent Antibody Technique ; In Situ Hybridization ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Molecular Sequence Data ; Neurons/physiology ; Octopamine/metabolism ; Polychlorinated Biphenyls/pharmacology ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Transport/drug effects ; Protein Transport/physiology ; Reserpine/pharmacology ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Homology, Amino Acid ; Serotonin/metabolism ; Vesicular Biogenic Amine Transport Proteins ; Vesicular Monoamine Transport Proteins
Chemical Substances	Adrenergic Uptake Inhibitors ; Membrane Glycoproteins ; Membrane Transport Proteins ; Protein Isoforms ; Vesicular Biogenic Amine Transport Proteins ; Vesicular Monoamine Transport Proteins ; Octopamine (14O50WS8JD) ; Serotonin (333DO1RDJY) ; Reserpine (8B1QWR724A) ; Polychlorinated Biphenyls (DFC2HB4I0K) ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2005-09-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	300903-8
ISSN	1097-4695 ; 0022-3034
ISSN (online)	1097-4695
ISSN	0022-3034
DOI	10.1002/neu.20146
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