ENaC structure and function in the wake of a resolved structure of a family member
Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the abil...
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| Veröffentlicht in: | American journal of physiology. Renal physiology 2011-10, Vol.301 (4), p.F684-F696 |
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| container_end_page | F696 |
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| container_title | American journal of physiology. Renal physiology |
| container_volume | 301 |
| creator | Kashlan, Ossama B Kleyman, Thomas R |
| description | Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the ability of these channels to sense the external environment. The absence of intracellular structures precludes insight into important interactions with intracellular factors that regulate trafficking and function. The primary sequences of ASIC1 and ENaC subunits are well conserved within the regions that are within or in close proximity to the plasma membrane, but poorly conserved in peripheral domains that may functionally differentiate family members. This review examines functional data, including ion selectivity, gating, and amiloride block, in light of the resolved ASIC1 structure. |
| doi_str_mv | 10.1152/ajprenal.00259.2011 |
| format | Article |
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Renal physiology</title><addtitle>Am J Physiol Renal Physiol</addtitle><description>Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the ability of these channels to sense the external environment. The absence of intracellular structures precludes insight into important interactions with intracellular factors that regulate trafficking and function. The primary sequences of ASIC1 and ENaC subunits are well conserved within the regions that are within or in close proximity to the plasma membrane, but poorly conserved in peripheral domains that may functionally differentiate family members. This review examines functional data, including ion selectivity, gating, and amiloride block, in light of the resolved ASIC1 structure.</description><subject>Acid Sensing Ion Channels</subject><subject>Amiloride - pharmacology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Chlorides - physiology</subject><subject>Conserved Sequence</subject><subject>Diuretics</subject><subject>Epithelial Sodium Channels - drug effects</subject><subject>Epithelial Sodium Channels - physiology</subject><subject>Humans</subject><subject>Ion Channel Gating - drug effects</subject><subject>Ion Channel Gating - physiology</subject><subject>Ions</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - drug effects</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Physiology</subject><subject>Plasma</subject><subject>Rats</subject><subject>Reviews</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sodium Channel Blockers - pharmacology</subject><subject>Sodium Channels - drug effects</subject><subject>Sodium Channels - physiology</subject><subject>Structure-Activity Relationship</subject><issn>1931-857X</issn><issn>1522-1466</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUdtKAzEQDaLYWv0CQYLvWyfJ3vIiSKkXKAqi4FuY3U3s1r3UZLfSv3e3N5R5mCFzzslwDiGXDMaMBfwGF0urKyzGADyQYw6MHZFht-Ee88PwuJulYF4cRB8DcubcAqCDcHZKBpxFgYBIDMnr9Bkn1DW2TZvWaopVRk1bpU1eVzSvaDPX9Ae_NK0NRWq1q4uVzv4QNu8Gy7xY01KXibbn5MRg4fTFro_I-_30bfLozV4eniZ3My_1ZdR4PiJwCJLAl-AjJCGXXIoUIUo4amOYyXyIWMyyKDVZkkHUFU8yYSDEOIjFiNxudZdtUuos1VVjsVBLm5do16rGXP3fVPlcfdYrJZhkMfQC1zsBW3-32jVqUbe2c9SpWIayM5X3ILEFpbZ2zmpz-ICB6nNQ-xzUJgfV59Cxrv7eduDsjRe_WymGyQ</recordid><startdate>20111001</startdate><enddate>20111001</enddate><creator>Kashlan, Ossama B</creator><creator>Kleyman, Thomas R</creator><general>American Physiological Society</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>5PM</scope></search><sort><creationdate>20111001</creationdate><title>ENaC structure and function in the wake of a resolved structure of a family member</title><author>Kashlan, Ossama B ; Kleyman, Thomas R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-4aa0205b54904a0b629293ca07b2aeff1fd407181d7cfdbd070702bd3f06a8583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Acid Sensing Ion Channels</topic><topic>Amiloride - pharmacology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Chlorides - physiology</topic><topic>Conserved Sequence</topic><topic>Diuretics</topic><topic>Epithelial Sodium Channels - drug effects</topic><topic>Epithelial Sodium Channels - physiology</topic><topic>Humans</topic><topic>Ion Channel Gating - drug effects</topic><topic>Ion Channel Gating - physiology</topic><topic>Ions</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - drug effects</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Physiology</topic><topic>Plasma</topic><topic>Rats</topic><topic>Reviews</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sodium Channel Blockers - pharmacology</topic><topic>Sodium Channels - drug effects</topic><topic>Sodium Channels - physiology</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kashlan, Ossama B</creatorcontrib><creatorcontrib>Kleyman, Thomas R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>American journal of physiology. Renal physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kashlan, Ossama B</au><au>Kleyman, Thomas R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ENaC structure and function in the wake of a resolved structure of a family member</atitle><jtitle>American journal of physiology. Renal physiology</jtitle><addtitle>Am J Physiol Renal Physiol</addtitle><date>2011-10-01</date><risdate>2011</risdate><volume>301</volume><issue>4</issue><spage>F684</spage><epage>F696</epage><pages>F684-F696</pages><issn>1931-857X</issn><eissn>1522-1466</eissn><abstract>Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the ability of these channels to sense the external environment. The absence of intracellular structures precludes insight into important interactions with intracellular factors that regulate trafficking and function. The primary sequences of ASIC1 and ENaC subunits are well conserved within the regions that are within or in close proximity to the plasma membrane, but poorly conserved in peripheral domains that may functionally differentiate family members. This review examines functional data, including ion selectivity, gating, and amiloride block, in light of the resolved ASIC1 structure.</abstract><cop>United States</cop><pub>American Physiological Society</pub><pmid>21753073</pmid><doi>10.1152/ajprenal.00259.2011</doi><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1931-857X |
| ispartof | American journal of physiology. Renal physiology, 2011-10, Vol.301 (4), p.F684-F696 |
| issn | 1931-857X 1522-1466 |
| language | eng |
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| source | MEDLINE; American Physiological Society Paid; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Acid Sensing Ion Channels Amiloride - pharmacology Amino Acid Sequence Animals Chlorides - physiology Conserved Sequence Diuretics Epithelial Sodium Channels - drug effects Epithelial Sodium Channels - physiology Humans Ion Channel Gating - drug effects Ion Channel Gating - physiology Ions Mice Molecular Sequence Data Nerve Tissue Proteins - drug effects Nerve Tissue Proteins - physiology Physiology Plasma Rats Reviews Sequence Homology, Amino Acid Sodium Channel Blockers - pharmacology Sodium Channels - drug effects Sodium Channels - physiology Structure-Activity Relationship |
| title | ENaC structure and function in the wake of a resolved structure of a family member |
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