Histidine-419 plays a role in energy coupling in the vesicular monoamine transporter from rat
Vesicular monoamine transporters (VMAT) catalyze transport of serotonin, dopamine, epinephrine and norepinephrine into subcellular storage organelles in a variety of cells. Accumulation of the neurotransmitter depends on the proton electrochemical gradient across the organelle membrane and involves...
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| Veröffentlicht in: | FEBS letters 1994-12, Vol.356 (1), p.145-150 |
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| creator | Shirvan, Anat Laskar, Orly Steiner-Mordoch, Sonia Schuldiner, Shimon |
| description | Vesicular monoamine transporters (VMAT) catalyze transport of serotonin, dopamine, epinephrine and norepinephrine into subcellular storage organelles in a variety of cells. Accumulation of the neurotransmitter depends on the proton electrochemical gradient across the organelle membrane and involves VMAT-mediated exchange of two lumenal protons with one cytoplasmic amine. It has been suggested in the past that His residues play a role in H
+ movement or in its coupling to active transport in H
+-symporters and antiporters. Indeed VMAT-mediated transport is inhibited by reagents specific for His residues. We have identified one His residue in VMAT1 from rat which is conserved in other vesicular neurotransmitter transporters. Mutagenesis of this His (H419) to either Arg or Cys completely inhibits [
3H]serotonin and [
3H]dopamine accumulation. Mutagenesis also inhibits other H
+-dependent partial reactions of VMAT such as the acceleration of binding of the high affinity ligand reserpine, but does not inhibit the [
3H]reserpine binding which is not dependent on H
+ translocation. It is concluded that His-419 plays a role in energy coupling in r-VMAT1. |
| doi_str_mv | 10.1016/0014-5793(94)01252-0 |
| format | Article |
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+ movement or in its coupling to active transport in H
+-symporters and antiporters. Indeed VMAT-mediated transport is inhibited by reagents specific for His residues. We have identified one His residue in VMAT1 from rat which is conserved in other vesicular neurotransmitter transporters. Mutagenesis of this His (H419) to either Arg or Cys completely inhibits [
3H]serotonin and [
3H]dopamine accumulation. Mutagenesis also inhibits other H
+-dependent partial reactions of VMAT such as the acceleration of binding of the high affinity ligand reserpine, but does not inhibit the [
3H]reserpine binding which is not dependent on H
+ translocation. It is concluded that His-419 plays a role in energy coupling in r-VMAT1.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(94)01252-0</identifier><identifier>PMID: 7988710</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Antiporter ; Arginine - metabolism ; Biological Transport ; CCCP, carbonyl cyanide m-chlorophenyl hydrazone ; Cysteine - metabolism ; DEPC, diethyl pyrocarbonate ; Drug resistance ; Energy coupling ; Energy Metabolism ; Glycoproteins - genetics ; Glycoproteins - metabolism ; H + transport ; Histidine ; Histidine - metabolism ; Membrane Glycoproteins ; Membrane Transport Proteins ; Mutagenesis, Site-Directed ; Neuropeptides ; Neurotransmitter Agents - genetics ; Neurotransmitter Agents - metabolism ; Neurotransmitter transport ; PG, phenylglyoxal ; Rats ; Reserpine - metabolism ; Serotonin - metabolism ; TEXANS ; Vesicular Biogenic Amine Transport Proteins ; Vesicular Monoamine Transport Proteins ; VMAT, vesicular monoamine transporter ; ΔμH+, electrochemical potential for H</subject><ispartof>FEBS letters, 1994-12, Vol.356 (1), p.145-150</ispartof><rights>1994</rights><rights>FEBS Letters 356 (1994) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5630-fe714ca2ed850c70c0b61d77bb3b958dca855fcc543afebc6787df57a37a5d6a3</citedby><cites>FETCH-LOGICAL-c5630-fe714ca2ed850c70c0b61d77bb3b958dca855fcc543afebc6787df57a37a5d6a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(94)01252-0$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7988710$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shirvan, Anat</creatorcontrib><creatorcontrib>Laskar, Orly</creatorcontrib><creatorcontrib>Steiner-Mordoch, Sonia</creatorcontrib><creatorcontrib>Schuldiner, Shimon</creatorcontrib><title>Histidine-419 plays a role in energy coupling in the vesicular monoamine transporter from rat</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Vesicular monoamine transporters (VMAT) catalyze transport of serotonin, dopamine, epinephrine and norepinephrine into subcellular storage organelles in a variety of cells. Accumulation of the neurotransmitter depends on the proton electrochemical gradient across the organelle membrane and involves VMAT-mediated exchange of two lumenal protons with one cytoplasmic amine. It has been suggested in the past that His residues play a role in H
+ movement or in its coupling to active transport in H
+-symporters and antiporters. Indeed VMAT-mediated transport is inhibited by reagents specific for His residues. We have identified one His residue in VMAT1 from rat which is conserved in other vesicular neurotransmitter transporters. Mutagenesis of this His (H419) to either Arg or Cys completely inhibits [
3H]serotonin and [
3H]dopamine accumulation. Mutagenesis also inhibits other H
+-dependent partial reactions of VMAT such as the acceleration of binding of the high affinity ligand reserpine, but does not inhibit the [
3H]reserpine binding which is not dependent on H
+ translocation. It is concluded that His-419 plays a role in energy coupling in r-VMAT1.</description><subject>Animals</subject><subject>Antiporter</subject><subject>Arginine - metabolism</subject><subject>Biological Transport</subject><subject>CCCP, carbonyl cyanide m-chlorophenyl hydrazone</subject><subject>Cysteine - metabolism</subject><subject>DEPC, diethyl pyrocarbonate</subject><subject>Drug resistance</subject><subject>Energy coupling</subject><subject>Energy Metabolism</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>H + transport</subject><subject>Histidine</subject><subject>Histidine - metabolism</subject><subject>Membrane Glycoproteins</subject><subject>Membrane Transport Proteins</subject><subject>Mutagenesis, Site-Directed</subject><subject>Neuropeptides</subject><subject>Neurotransmitter Agents - genetics</subject><subject>Neurotransmitter Agents - metabolism</subject><subject>Neurotransmitter transport</subject><subject>PG, phenylglyoxal</subject><subject>Rats</subject><subject>Reserpine - metabolism</subject><subject>Serotonin - metabolism</subject><subject>TEXANS</subject><subject>Vesicular Biogenic Amine Transport Proteins</subject><subject>Vesicular Monoamine Transport Proteins</subject><subject>VMAT, vesicular monoamine transporter</subject><subject>ΔμH+, electrochemical potential for H</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtKxDAUhoMoOo6-gUJWootq0iZNuhF0cFQQ3OhSQpqcaqRtatIq8_a2zuBSXIX8Nw4fQkeUnFNC8wtCKEu4KLLTgp0RmvI0IVtoRqXIkozlchvNfiN7aD_GdzL-JS120a4opBSUzNDLnYu9s66FhNECd7VeRaxx8DVg12JoIbyusPFDV7v2dZL6N8CfEJ0Zah1w41uvm7GO-6Db2PnQQ8BV8A0Ouj9AO5WuIxxu3jl6Xt48Le6Sh8fb-8XVQ2J4npGkAkGZ0SlYyYkRxJAyp1aIsszKgktrtOS8MoazTFdQmlxIYSsudCY0t7nO5uhkvdsF_zFA7FXjooG61i34ISqaixELT8cgWwdN8DEGqFQXXKPDSlGiJqpqQqYmZKpg6oeqImPteLM_lA3Y39IG4-gv1_6Xq2H1r021vLlOJ2PSC_ajTkOX6yEYaX06CCoaB60B6wKYXlnv_r70Gyovmp4</recordid><startdate>19941214</startdate><enddate>19941214</enddate><creator>Shirvan, Anat</creator><creator>Laskar, Orly</creator><creator>Steiner-Mordoch, Sonia</creator><creator>Schuldiner, Shimon</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope></search><sort><creationdate>19941214</creationdate><title>Histidine-419 plays a role in energy coupling in the vesicular monoamine transporter from rat</title><author>Shirvan, Anat ; Laskar, Orly ; Steiner-Mordoch, Sonia ; Schuldiner, Shimon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5630-fe714ca2ed850c70c0b61d77bb3b958dca855fcc543afebc6787df57a37a5d6a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Antiporter</topic><topic>Arginine - metabolism</topic><topic>Biological Transport</topic><topic>CCCP, carbonyl cyanide m-chlorophenyl hydrazone</topic><topic>Cysteine - metabolism</topic><topic>DEPC, diethyl pyrocarbonate</topic><topic>Drug resistance</topic><topic>Energy coupling</topic><topic>Energy Metabolism</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - metabolism</topic><topic>H + transport</topic><topic>Histidine</topic><topic>Histidine - metabolism</topic><topic>Membrane Glycoproteins</topic><topic>Membrane Transport Proteins</topic><topic>Mutagenesis, Site-Directed</topic><topic>Neuropeptides</topic><topic>Neurotransmitter Agents - genetics</topic><topic>Neurotransmitter Agents - metabolism</topic><topic>Neurotransmitter transport</topic><topic>PG, phenylglyoxal</topic><topic>Rats</topic><topic>Reserpine - metabolism</topic><topic>Serotonin - metabolism</topic><topic>TEXANS</topic><topic>Vesicular Biogenic Amine Transport Proteins</topic><topic>Vesicular Monoamine Transport Proteins</topic><topic>VMAT, vesicular monoamine transporter</topic><topic>ΔμH+, electrochemical potential for H</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shirvan, Anat</creatorcontrib><creatorcontrib>Laskar, Orly</creatorcontrib><creatorcontrib>Steiner-Mordoch, Sonia</creatorcontrib><creatorcontrib>Schuldiner, Shimon</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shirvan, Anat</au><au>Laskar, Orly</au><au>Steiner-Mordoch, Sonia</au><au>Schuldiner, Shimon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Histidine-419 plays a role in energy coupling in the vesicular monoamine transporter from rat</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1994-12-14</date><risdate>1994</risdate><volume>356</volume><issue>1</issue><spage>145</spage><epage>150</epage><pages>145-150</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Vesicular monoamine transporters (VMAT) catalyze transport of serotonin, dopamine, epinephrine and norepinephrine into subcellular storage organelles in a variety of cells. Accumulation of the neurotransmitter depends on the proton electrochemical gradient across the organelle membrane and involves VMAT-mediated exchange of two lumenal protons with one cytoplasmic amine. It has been suggested in the past that His residues play a role in H
+ movement or in its coupling to active transport in H
+-symporters and antiporters. Indeed VMAT-mediated transport is inhibited by reagents specific for His residues. We have identified one His residue in VMAT1 from rat which is conserved in other vesicular neurotransmitter transporters. Mutagenesis of this His (H419) to either Arg or Cys completely inhibits [
3H]serotonin and [
3H]dopamine accumulation. Mutagenesis also inhibits other H
+-dependent partial reactions of VMAT such as the acceleration of binding of the high affinity ligand reserpine, but does not inhibit the [
3H]reserpine binding which is not dependent on H
+ translocation. It is concluded that His-419 plays a role in energy coupling in r-VMAT1.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7988710</pmid><doi>10.1016/0014-5793(94)01252-0</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1994-12, Vol.356 (1), p.145-150 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Antiporter Arginine - metabolism Biological Transport CCCP, carbonyl cyanide m-chlorophenyl hydrazone Cysteine - metabolism DEPC, diethyl pyrocarbonate Drug resistance Energy coupling Energy Metabolism Glycoproteins - genetics Glycoproteins - metabolism H + transport Histidine Histidine - metabolism Membrane Glycoproteins Membrane Transport Proteins Mutagenesis, Site-Directed Neuropeptides Neurotransmitter Agents - genetics Neurotransmitter Agents - metabolism Neurotransmitter transport PG, phenylglyoxal Rats Reserpine - metabolism Serotonin - metabolism TEXANS Vesicular Biogenic Amine Transport Proteins Vesicular Monoamine Transport Proteins VMAT, vesicular monoamine transporter ΔμH+, electrochemical potential for H |
| title | Histidine-419 plays a role in energy coupling in the vesicular monoamine transporter from rat |
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