A tyrosine residue in TM6 of the Vanilloid Receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents
The Vanilloid Receptor TRPV1 is a non-selective cation channel with a high relative Ca 2+ permeability. TRPV1 exhibits slow desensitization, a potential mechanism regulating adaptation of peripheral sensory neurons to noxious stimuli. The predicted folding pattern of TRPV1 resembles that of voltage-...
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| Veröffentlicht in: | Molecular and cellular neuroscience 2003-06, Vol.23 (2), p.314-324 |
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| creator | Mohapatra, Durga Prasanna Wang, Sho-Ya Wang, Ging Kuo Nau, Carla |
| description | The Vanilloid Receptor TRPV1 is a non-selective cation channel with a high relative Ca
2+ permeability. TRPV1 exhibits slow desensitization, a potential mechanism regulating adaptation of peripheral sensory neurons to noxious stimuli. The predicted folding pattern of TRPV1 resembles that of voltage-gated channels. Sequence alignment of segments 6 of TRPV1 and voltage-gated Na
+ channels reveals a conserved aromatic amino acid that in Na
+ channels is involved in fast inactivation and pharmacological block. We found that replacing this tyrosine Y671 by positively charged lysine (K) completely abrogated Ca
2+-dependent desensitization. Y671K also exhibited significant reduction in Ca
2+ permeability that was not responsible for the lack in desensitization. Substitution of Y671 with negatively charged aspartate or uncharged alanine slightly altered desensitization but left Ca
2+ permeability unchanged. Substitution of Y671 with positively charged arginine produced a phenotype similar to Y671K. We propose that residue Y671 is critical for the high relative Ca
2+ permeability of TRPV1 and participates in the structural rearrangements of the channel protein leading to Ca
2+-dependent desensitization. |
| doi_str_mv | 10.1016/S1044-7431(03)00054-X |
| format | Article |
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2+ permeability. TRPV1 exhibits slow desensitization, a potential mechanism regulating adaptation of peripheral sensory neurons to noxious stimuli. The predicted folding pattern of TRPV1 resembles that of voltage-gated channels. Sequence alignment of segments 6 of TRPV1 and voltage-gated Na
+ channels reveals a conserved aromatic amino acid that in Na
+ channels is involved in fast inactivation and pharmacological block. We found that replacing this tyrosine Y671 by positively charged lysine (K) completely abrogated Ca
2+-dependent desensitization. Y671K also exhibited significant reduction in Ca
2+ permeability that was not responsible for the lack in desensitization. Substitution of Y671 with negatively charged aspartate or uncharged alanine slightly altered desensitization but left Ca
2+ permeability unchanged. Substitution of Y671 with positively charged arginine produced a phenotype similar to Y671K. We propose that residue Y671 is critical for the high relative Ca
2+ permeability of TRPV1 and participates in the structural rearrangements of the channel protein leading to Ca
2+-dependent desensitization.</description><identifier>ISSN: 1044-7431</identifier><identifier>EISSN: 1095-9327</identifier><identifier>DOI: 10.1016/S1044-7431(03)00054-X</identifier><identifier>PMID: 12812762</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence - genetics ; Amino Acids - genetics ; Amino Acids - metabolism ; Calcium Signaling - drug effects ; Calcium Signaling - genetics ; Capsaicin - pharmacology ; capsaicin receptors ; Cell Line ; Cell Membrane - genetics ; Cell Membrane - metabolism ; Humans ; Membrane Potentials - genetics ; Mutation - genetics ; Neurons, Afferent - metabolism ; Nociceptors - metabolism ; Pain - genetics ; Pain - metabolism ; Protein Structure, Tertiary - genetics ; Protons ; Receptors, Drug - drug effects ; Receptors, Drug - genetics ; Receptors, Drug - metabolism ; Sodium Channels - drug effects ; Sodium Channels - genetics ; Sodium Channels - metabolism ; Tyrosine - metabolism</subject><ispartof>Molecular and cellular neuroscience, 2003-06, Vol.23 (2), p.314-324</ispartof><rights>2003 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-410ed6bf05a99eb06e1e47450dbcda4de3ddbaeb9edccb54e4b25c6f698f990c3</citedby><cites>FETCH-LOGICAL-c536t-410ed6bf05a99eb06e1e47450dbcda4de3ddbaeb9edccb54e4b25c6f698f990c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S104474310300054X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12812762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mohapatra, Durga Prasanna</creatorcontrib><creatorcontrib>Wang, Sho-Ya</creatorcontrib><creatorcontrib>Wang, Ging Kuo</creatorcontrib><creatorcontrib>Nau, Carla</creatorcontrib><title>A tyrosine residue in TM6 of the Vanilloid Receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents</title><title>Molecular and cellular neuroscience</title><addtitle>Mol Cell Neurosci</addtitle><description>The Vanilloid Receptor TRPV1 is a non-selective cation channel with a high relative Ca
2+ permeability. TRPV1 exhibits slow desensitization, a potential mechanism regulating adaptation of peripheral sensory neurons to noxious stimuli. The predicted folding pattern of TRPV1 resembles that of voltage-gated channels. Sequence alignment of segments 6 of TRPV1 and voltage-gated Na
+ channels reveals a conserved aromatic amino acid that in Na
+ channels is involved in fast inactivation and pharmacological block. We found that replacing this tyrosine Y671 by positively charged lysine (K) completely abrogated Ca
2+-dependent desensitization. Y671K also exhibited significant reduction in Ca
2+ permeability that was not responsible for the lack in desensitization. Substitution of Y671 with negatively charged aspartate or uncharged alanine slightly altered desensitization but left Ca
2+ permeability unchanged. Substitution of Y671 with positively charged arginine produced a phenotype similar to Y671K. We propose that residue Y671 is critical for the high relative Ca
2+ permeability of TRPV1 and participates in the structural rearrangements of the channel protein leading to Ca
2+-dependent desensitization.</description><subject>Amino Acid Sequence - genetics</subject><subject>Amino Acids - genetics</subject><subject>Amino Acids - metabolism</subject><subject>Calcium Signaling - drug effects</subject><subject>Calcium Signaling - genetics</subject><subject>Capsaicin - pharmacology</subject><subject>capsaicin receptors</subject><subject>Cell Line</subject><subject>Cell Membrane - genetics</subject><subject>Cell Membrane - metabolism</subject><subject>Humans</subject><subject>Membrane Potentials - genetics</subject><subject>Mutation - genetics</subject><subject>Neurons, Afferent - metabolism</subject><subject>Nociceptors - metabolism</subject><subject>Pain - genetics</subject><subject>Pain - metabolism</subject><subject>Protein Structure, Tertiary - genetics</subject><subject>Protons</subject><subject>Receptors, Drug - drug effects</subject><subject>Receptors, Drug - genetics</subject><subject>Receptors, Drug - metabolism</subject><subject>Sodium Channels - drug effects</subject><subject>Sodium Channels - genetics</subject><subject>Sodium Channels - metabolism</subject><subject>Tyrosine - metabolism</subject><issn>1044-7431</issn><issn>1095-9327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctu1TAQhiMEohd4BJBXiC4CduxcvEJV1QJSK1A5VN1ZvkzEoMQOtnOk04fgmUl6jsSyq5nF9_8jzVcUbxj9wChrPv5gVIiyFZy9p_yMUlqL8v5ZccyorEvJq_b5uh-Qo-Ikpd8rVEn-sjhiVceqtqmOi7_nJO9iSOiBREjoZiDoyeamIaEn-ReQO-1xGAI6cgsWphwi2dx-v2MLtg3DFtzKO0jgE2Z80BmDJ9o7YvVgcR7JBHEEbXDAvFtLrZ6SRou-1DbjVuelws4xgs_pVfGi10OC14d5Wvy8utxcfCmvv33-enF-XdqaN7kUjIJrTE9rLSUY2gAD0YqaOmOdFg64c0aDkeCsNbUAYaraNn0ju15Kavlp8W7fO8XwZ4aU1YjJwjBoD2FOquW87VrZPgmyTvKuomwB6z1ol2-mCL2aIo467hSjajWmHo2pVYeiXD0aU_dL7u3hwGxGcP9TB0UL8GkPwPKPLUJUySJ4Cw4j2KxcwCdO_AMOc6mC</recordid><startdate>20030601</startdate><enddate>20030601</enddate><creator>Mohapatra, Durga Prasanna</creator><creator>Wang, Sho-Ya</creator><creator>Wang, Ging Kuo</creator><creator>Nau, Carla</creator><general>Elsevier Inc</general><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><scope>7X8</scope></search><sort><creationdate>20030601</creationdate><title>A tyrosine residue in TM6 of the Vanilloid Receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents</title><author>Mohapatra, Durga Prasanna ; Wang, Sho-Ya ; Wang, Ging Kuo ; Nau, Carla</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-410ed6bf05a99eb06e1e47450dbcda4de3ddbaeb9edccb54e4b25c6f698f990c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence - genetics</topic><topic>Amino Acids - genetics</topic><topic>Amino Acids - metabolism</topic><topic>Calcium Signaling - drug effects</topic><topic>Calcium Signaling - genetics</topic><topic>Capsaicin - pharmacology</topic><topic>capsaicin receptors</topic><topic>Cell Line</topic><topic>Cell Membrane - genetics</topic><topic>Cell Membrane - metabolism</topic><topic>Humans</topic><topic>Membrane Potentials - genetics</topic><topic>Mutation - genetics</topic><topic>Neurons, Afferent - metabolism</topic><topic>Nociceptors - metabolism</topic><topic>Pain - genetics</topic><topic>Pain - metabolism</topic><topic>Protein Structure, Tertiary - genetics</topic><topic>Protons</topic><topic>Receptors, Drug - drug effects</topic><topic>Receptors, Drug - genetics</topic><topic>Receptors, Drug - metabolism</topic><topic>Sodium Channels - drug effects</topic><topic>Sodium Channels - genetics</topic><topic>Sodium Channels - metabolism</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mohapatra, Durga Prasanna</creatorcontrib><creatorcontrib>Wang, Sho-Ya</creatorcontrib><creatorcontrib>Wang, Ging Kuo</creatorcontrib><creatorcontrib>Nau, Carla</creatorcontrib><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><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mohapatra, Durga Prasanna</au><au>Wang, Sho-Ya</au><au>Wang, Ging Kuo</au><au>Nau, Carla</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A tyrosine residue in TM6 of the Vanilloid Receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents</atitle><jtitle>Molecular and cellular neuroscience</jtitle><addtitle>Mol Cell Neurosci</addtitle><date>2003-06-01</date><risdate>2003</risdate><volume>23</volume><issue>2</issue><spage>314</spage><epage>324</epage><pages>314-324</pages><issn>1044-7431</issn><eissn>1095-9327</eissn><abstract>The Vanilloid Receptor TRPV1 is a non-selective cation channel with a high relative Ca
2+ permeability. TRPV1 exhibits slow desensitization, a potential mechanism regulating adaptation of peripheral sensory neurons to noxious stimuli. The predicted folding pattern of TRPV1 resembles that of voltage-gated channels. Sequence alignment of segments 6 of TRPV1 and voltage-gated Na
+ channels reveals a conserved aromatic amino acid that in Na
+ channels is involved in fast inactivation and pharmacological block. We found that replacing this tyrosine Y671 by positively charged lysine (K) completely abrogated Ca
2+-dependent desensitization. Y671K also exhibited significant reduction in Ca
2+ permeability that was not responsible for the lack in desensitization. Substitution of Y671 with negatively charged aspartate or uncharged alanine slightly altered desensitization but left Ca
2+ permeability unchanged. Substitution of Y671 with positively charged arginine produced a phenotype similar to Y671K. We propose that residue Y671 is critical for the high relative Ca
2+ permeability of TRPV1 and participates in the structural rearrangements of the channel protein leading to Ca
2+-dependent desensitization.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12812762</pmid><doi>10.1016/S1044-7431(03)00054-X</doi><tpages>11</tpages></addata></record> |
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| subjects | Amino Acid Sequence - genetics Amino Acids - genetics Amino Acids - metabolism Calcium Signaling - drug effects Calcium Signaling - genetics Capsaicin - pharmacology capsaicin receptors Cell Line Cell Membrane - genetics Cell Membrane - metabolism Humans Membrane Potentials - genetics Mutation - genetics Neurons, Afferent - metabolism Nociceptors - metabolism Pain - genetics Pain - metabolism Protein Structure, Tertiary - genetics Protons Receptors, Drug - drug effects Receptors, Drug - genetics Receptors, Drug - metabolism Sodium Channels - drug effects Sodium Channels - genetics Sodium Channels - metabolism Tyrosine - metabolism |
| title | A tyrosine residue in TM6 of the Vanilloid Receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents |
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