Cryo-EM structures of the ATP release channel pannexin 1
The plasma membrane adenosine triphosphate (ATP) release channel pannexin 1 (PANX1) has been implicated in many physiological and pathophysiological processes associated with purinergic signaling, including cancer progression, apoptotic cell clearance, inflammation, blood pressure regulation, oocyte...
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| Veröffentlicht in: | Nature structural & molecular biology 2020-04, Vol.27 (4), p.373-381 |
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| creator | Deng, Zengqin He, Zhihui Maksaev, Grigory Bitter, Ryan M. Rau, Michael Fitzpatrick, James A. J. Yuan, Peng |
| description | The plasma membrane adenosine triphosphate (ATP) release channel pannexin 1 (PANX1) has been implicated in many physiological and pathophysiological processes associated with purinergic signaling, including cancer progression, apoptotic cell clearance, inflammation, blood pressure regulation, oocyte development, epilepsy and neuropathic pain. Here we present near-atomic-resolution structures of human and frog PANX1 determined by cryo-electron microscopy that revealed a heptameric channel architecture. Compatible with ATP permeation, the transmembrane pore and cytoplasmic vestibule were exceptionally wide. An extracellular tryptophan ring located at the outer pore created a constriction site, potentially functioning as a molecular sieve that restricts the size of permeable substrates. The amino and carboxyl termini, not resolved in the density map, appeared to be structurally dynamic and might contribute to narrowing of the pore during channel gating. In combination with functional characterization, this work elucidates the previously unknown architecture of pannexin channels and establishes a foundation for understanding their unique channel properties.
Cryo-EM structures of plasma membrane ATP release channel pannexin 1 reveal heptameric architecture, wide pore and a constriction potentially restricting the size of permeable substrates. Combined with functional assays, they offer insights into channel gating. |
| doi_str_mv | 10.1038/s41594-020-0401-0 |
| format | Article |
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Cryo-EM structures of plasma membrane ATP release channel pannexin 1 reveal heptameric architecture, wide pore and a constriction potentially restricting the size of permeable substrates. Combined with functional assays, they offer insights into channel gating.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/s41594-020-0401-0</identifier><identifier>PMID: 32231289</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/1647/2204/1453 ; 631/45/612/1237 ; 631/535/1258/1259 ; 631/57/2270/1140 ; Adenosine triphosphate ; Adenosine Triphosphate - chemistry ; Adenosine Triphosphate - genetics ; Animals ; Anura - genetics ; Apoptosis ; Architecture ; ATP ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Blood pressure ; Cell Membrane - chemistry ; Cell Membrane - genetics ; Cell Membrane - ultrastructure ; Channel gating ; Connexins - chemistry ; Connexins - genetics ; Connexins - ultrastructure ; Constrictions ; Cryoelectron Microscopy ; Electron microscopy ; Epilepsy ; Gametocytes ; Humans ; Life Sciences ; Membrane Biology ; Membranes ; Molecular sieves ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - ultrastructure ; Neuralgia ; Permeability ; Protein Conformation ; Protein Structure ; Signal Transduction - genetics ; Substrates ; Tryptophan ; Vestibules</subject><ispartof>Nature structural & molecular biology, 2020-04, Vol.27 (4), p.373-381</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2020</rights><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2020.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c481t-8c7d3de74d6200389e9a197aea4c66c74b103ba7a8054a582ff67928d93508513</citedby><cites>FETCH-LOGICAL-c481t-8c7d3de74d6200389e9a197aea4c66c74b103ba7a8054a582ff67928d93508513</cites><orcidid>0000-0002-5660-225X ; 0000-0003-4184-8377 ; 0000-0001-6242-1634 ; 0000-0002-5658-2068 ; 0000-0002-7907-3602 ; 0000-0001-5170-2000</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41594-020-0401-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41594-020-0401-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32231289$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Deng, Zengqin</creatorcontrib><creatorcontrib>He, Zhihui</creatorcontrib><creatorcontrib>Maksaev, Grigory</creatorcontrib><creatorcontrib>Bitter, Ryan M.</creatorcontrib><creatorcontrib>Rau, Michael</creatorcontrib><creatorcontrib>Fitzpatrick, James A. J.</creatorcontrib><creatorcontrib>Yuan, Peng</creatorcontrib><title>Cryo-EM structures of the ATP release channel pannexin 1</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>The plasma membrane adenosine triphosphate (ATP) release channel pannexin 1 (PANX1) has been implicated in many physiological and pathophysiological processes associated with purinergic signaling, including cancer progression, apoptotic cell clearance, inflammation, blood pressure regulation, oocyte development, epilepsy and neuropathic pain. Here we present near-atomic-resolution structures of human and frog PANX1 determined by cryo-electron microscopy that revealed a heptameric channel architecture. Compatible with ATP permeation, the transmembrane pore and cytoplasmic vestibule were exceptionally wide. An extracellular tryptophan ring located at the outer pore created a constriction site, potentially functioning as a molecular sieve that restricts the size of permeable substrates. The amino and carboxyl termini, not resolved in the density map, appeared to be structurally dynamic and might contribute to narrowing of the pore during channel gating. In combination with functional characterization, this work elucidates the previously unknown architecture of pannexin channels and establishes a foundation for understanding their unique channel properties.
Cryo-EM structures of plasma membrane ATP release channel pannexin 1 reveal heptameric architecture, wide pore and a constriction potentially restricting the size of permeable substrates. Combined with functional assays, they offer insights into channel gating.</description><subject>631/1647/2204/1453</subject><subject>631/45/612/1237</subject><subject>631/535/1258/1259</subject><subject>631/57/2270/1140</subject><subject>Adenosine triphosphate</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Adenosine Triphosphate - genetics</subject><subject>Animals</subject><subject>Anura - genetics</subject><subject>Apoptosis</subject><subject>Architecture</subject><subject>ATP</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Blood pressure</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - genetics</subject><subject>Cell Membrane - ultrastructure</subject><subject>Channel gating</subject><subject>Connexins - chemistry</subject><subject>Connexins - genetics</subject><subject>Connexins - ultrastructure</subject><subject>Constrictions</subject><subject>Cryoelectron Microscopy</subject><subject>Electron microscopy</subject><subject>Epilepsy</subject><subject>Gametocytes</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Membranes</subject><subject>Molecular sieves</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - ultrastructure</subject><subject>Neuralgia</subject><subject>Permeability</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><subject>Signal Transduction - genetics</subject><subject>Substrates</subject><subject>Tryptophan</subject><subject>Vestibules</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kE1LAzEQhoMotlZ_gBdZ8OIlms8mOZZSP6Cih3oOaXbWtmx3a7IL9t-bZauC4GkG5sk7kwehS0puKeH6LgoqjcCEEUwEoZgcoSGVQmJjtDz-6Q0foLMYN4QwKRU_RQPOGKdMmyHS07Cv8ew5i01ofdMGiFldZM0KssniNQtQgouQ-ZWrKiizXVc-11VGz9FJ4coIF4c6Qm_3s8X0Ec9fHp6mkzn2QtMGa69ynoMS-ZiRdLMB46hRDpzw47FXYpl-snTKaSKFk5oVxVgZpnPDJdGS8hG66XN3of5oITZ2u44eytJVULfRMq4lU4ammBG6_oNu6jZU6bqOUsaotDlRtKd8qGMMUNhdWG9d2FtKbKfV9lpt0mo7rbZLvjokt8st5D8vvj0mgPVATKPqHcLv6v9TvwCf8n7j</recordid><startdate>20200401</startdate><enddate>20200401</enddate><creator>Deng, Zengqin</creator><creator>He, Zhihui</creator><creator>Maksaev, Grigory</creator><creator>Bitter, Ryan M.</creator><creator>Rau, Michael</creator><creator>Fitzpatrick, James A. 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J.</au><au>Yuan, Peng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cryo-EM structures of the ATP release channel pannexin 1</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2020-04-01</date><risdate>2020</risdate><volume>27</volume><issue>4</issue><spage>373</spage><epage>381</epage><pages>373-381</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>The plasma membrane adenosine triphosphate (ATP) release channel pannexin 1 (PANX1) has been implicated in many physiological and pathophysiological processes associated with purinergic signaling, including cancer progression, apoptotic cell clearance, inflammation, blood pressure regulation, oocyte development, epilepsy and neuropathic pain. Here we present near-atomic-resolution structures of human and frog PANX1 determined by cryo-electron microscopy that revealed a heptameric channel architecture. Compatible with ATP permeation, the transmembrane pore and cytoplasmic vestibule were exceptionally wide. An extracellular tryptophan ring located at the outer pore created a constriction site, potentially functioning as a molecular sieve that restricts the size of permeable substrates. The amino and carboxyl termini, not resolved in the density map, appeared to be structurally dynamic and might contribute to narrowing of the pore during channel gating. In combination with functional characterization, this work elucidates the previously unknown architecture of pannexin channels and establishes a foundation for understanding their unique channel properties.
Cryo-EM structures of plasma membrane ATP release channel pannexin 1 reveal heptameric architecture, wide pore and a constriction potentially restricting the size of permeable substrates. Combined with functional assays, they offer insights into channel gating.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>32231289</pmid><doi>10.1038/s41594-020-0401-0</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-5660-225X</orcidid><orcidid>https://orcid.org/0000-0003-4184-8377</orcidid><orcidid>https://orcid.org/0000-0001-6242-1634</orcidid><orcidid>https://orcid.org/0000-0002-5658-2068</orcidid><orcidid>https://orcid.org/0000-0002-7907-3602</orcidid><orcidid>https://orcid.org/0000-0001-5170-2000</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 631/1647/2204/1453 631/45/612/1237 631/535/1258/1259 631/57/2270/1140 Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - genetics Animals Anura - genetics Apoptosis Architecture ATP Biochemistry Biological Microscopy Biomedical and Life Sciences Blood pressure Cell Membrane - chemistry Cell Membrane - genetics Cell Membrane - ultrastructure Channel gating Connexins - chemistry Connexins - genetics Connexins - ultrastructure Constrictions Cryoelectron Microscopy Electron microscopy Epilepsy Gametocytes Humans Life Sciences Membrane Biology Membranes Molecular sieves Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - ultrastructure Neuralgia Permeability Protein Conformation Protein Structure Signal Transduction - genetics Substrates Tryptophan Vestibules |
| title | Cryo-EM structures of the ATP release channel pannexin 1 |
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