Mechanism of selectivity in aquaporins and aquaglyceroporins
Aquaporins and aquaglyceroporins form a family of pore proteins that facilitate the efficient and selective flux of small solutes across biological membranes. We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O₂, CO₂, NH₃, glycerol, urea, and water. U...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2008-01, Vol.105 (4), p.1198-1203 |
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| creator | Hub, Jochen S de Groot, Bert L |
| description | Aquaporins and aquaglyceroporins form a family of pore proteins that facilitate the efficient and selective flux of small solutes across biological membranes. We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O₂, CO₂, NH₃, glycerol, urea, and water. Using molecular dynamics simulations, we calculated potentials of mean force for solute permeation along the aquaporin channels and compared them with the alternative pathway across the lipid bilayer. For small solutes permeating through AQP1, a remarkable anticorrelation between permeability and solute hydrophobicity was observed, whereas the opposite trend was observed for permeation through the membrane. This finding renders AQP1 a selective filter for small polar solutes, whereas GlpF was found to be highly permeable for small solutes and permeable for larger solutes. Surprisingly, not solute-channel but water-channel interactions were found to be the key determinant underlying the selectivity mechanism of aquaporins. Hence, a hydrophobic effect, together with steric restraints, determines the selectivity of aquaporins. |
| doi_str_mv | 10.1073/pnas.0707662104 |
| format | Article |
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We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O₂, CO₂, NH₃, glycerol, urea, and water. Using molecular dynamics simulations, we calculated potentials of mean force for solute permeation along the aquaporin channels and compared them with the alternative pathway across the lipid bilayer. For small solutes permeating through AQP1, a remarkable anticorrelation between permeability and solute hydrophobicity was observed, whereas the opposite trend was observed for permeation through the membrane. This finding renders AQP1 a selective filter for small polar solutes, whereas GlpF was found to be highly permeable for small solutes and permeable for larger solutes. Surprisingly, not solute-channel but water-channel interactions were found to be the key determinant underlying the selectivity mechanism of aquaporins. Hence, a hydrophobic effect, together with steric restraints, determines the selectivity of aquaporins.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0707662104</identifier><identifier>PMID: 18202181</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Ammonia ; Ammonia - chemistry ; Animals ; Aquaglyceroporins ; Aquaglyceroporins - chemistry ; Aquaporin 1 - chemistry ; Aquaporin 1 - genetics ; Aquaporins ; Aquaporins - chemistry ; Atoms ; Biological Sciences ; Carbon Dioxide - chemistry ; Cattle ; Computational Biology - methods ; Escherichia coli Proteins - chemistry ; Glycerol - chemistry ; Humans ; Hydrogen bonds ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Lipid Bilayers - chemistry ; Membranes ; Molecular biology ; Molecular interactions ; Molecules ; Oxygen - chemistry ; Permeability ; Point Mutation ; Proteins ; Signal Transduction - physiology ; Solute movement ; Solutes ; Solutions ; Studies ; Thermodynamics ; Umbrellas ; Urea - chemistry ; Water - chemistry</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2008-01, Vol.105 (4), p.1198-1203</ispartof><rights>Copyright 2008 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jan 29, 2008</rights><rights>2008 by The National Academy of Sciences of the USA 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c616t-bcfd446de0865a57d528d228d3ec5cb931d9d597bed5961d668c69d509cab7203</citedby><cites>FETCH-LOGICAL-c616t-bcfd446de0865a57d528d228d3ec5cb931d9d597bed5961d668c69d509cab7203</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/105/4.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25451252$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25451252$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18202181$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hub, Jochen S</creatorcontrib><creatorcontrib>de Groot, Bert L</creatorcontrib><title>Mechanism of selectivity in aquaporins and aquaglyceroporins</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Aquaporins and aquaglyceroporins form a family of pore proteins that facilitate the efficient and selective flux of small solutes across biological membranes. We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O₂, CO₂, NH₃, glycerol, urea, and water. Using molecular dynamics simulations, we calculated potentials of mean force for solute permeation along the aquaporin channels and compared them with the alternative pathway across the lipid bilayer. For small solutes permeating through AQP1, a remarkable anticorrelation between permeability and solute hydrophobicity was observed, whereas the opposite trend was observed for permeation through the membrane. This finding renders AQP1 a selective filter for small polar solutes, whereas GlpF was found to be highly permeable for small solutes and permeable for larger solutes. Surprisingly, not solute-channel but water-channel interactions were found to be the key determinant underlying the selectivity mechanism of aquaporins. Hence, a hydrophobic effect, together with steric restraints, determines the selectivity of aquaporins.</description><subject>Ammonia</subject><subject>Ammonia - chemistry</subject><subject>Animals</subject><subject>Aquaglyceroporins</subject><subject>Aquaglyceroporins - chemistry</subject><subject>Aquaporin 1 - chemistry</subject><subject>Aquaporin 1 - genetics</subject><subject>Aquaporins</subject><subject>Aquaporins - chemistry</subject><subject>Atoms</subject><subject>Biological Sciences</subject><subject>Carbon Dioxide - chemistry</subject><subject>Cattle</subject><subject>Computational Biology - methods</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Glycerol - chemistry</subject><subject>Humans</subject><subject>Hydrogen bonds</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Lipid Bilayers - chemistry</subject><subject>Membranes</subject><subject>Molecular biology</subject><subject>Molecular interactions</subject><subject>Molecules</subject><subject>Oxygen - chemistry</subject><subject>Permeability</subject><subject>Point Mutation</subject><subject>Proteins</subject><subject>Signal Transduction - physiology</subject><subject>Solute movement</subject><subject>Solutes</subject><subject>Solutions</subject><subject>Studies</subject><subject>Thermodynamics</subject><subject>Umbrellas</subject><subject>Urea - chemistry</subject><subject>Water - chemistry</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxSMEotvCmRMQcYBT2hnHn1KFhCq-pCIO0LPlOM7Wq2y8tZOK_e_rJatuQUgcbMszv3ny8yuKFwinCKI-2wwmnYIAwTlBoI-KBYLCilMFj4sFABGVpIQeFccprQBAMQlPiyOUBAhKXBTn35y9NoNP6zJ0ZXK9s6O_9eO29ENpbiazCdEPqTRD-_u67LfWxTBXnxVPOtMn93x_nhRXnz7-vPhSXX7__PXiw2VlOfKxamzXUspbB5Izw0TLiGxJXrWzzDaqxla1TInG5Z1jy7m0PFdAWdMIAvVJ8X7W3UzN2rXWDWM0vd5EvzZxq4Px-s_O4K_1MtxqQmqKyLLA271ADDeTS6Ne-2Rd35vBhSlpAYQKCeq_IMkWkAvM4Ju_wFWY4pB_ITNY15QpmaGzGbIxpBRdd_9kBL3LT-_y04f88sSrh04P_D6wDLzbA7vJgxzTVCMqqbup70f3a3wg9W8yAy9nYJXGEO8JwihDwkjuv577nQnaLKNP-urHzhyAZDVyWd8BZ-PBgQ</recordid><startdate>20080129</startdate><enddate>20080129</enddate><creator>Hub, Jochen S</creator><creator>de Groot, Bert L</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080129</creationdate><title>Mechanism of selectivity in aquaporins and aquaglyceroporins</title><author>Hub, Jochen S ; de Groot, Bert L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c616t-bcfd446de0865a57d528d228d3ec5cb931d9d597bed5961d668c69d509cab7203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Ammonia</topic><topic>Ammonia - chemistry</topic><topic>Animals</topic><topic>Aquaglyceroporins</topic><topic>Aquaglyceroporins - chemistry</topic><topic>Aquaporin 1 - chemistry</topic><topic>Aquaporin 1 - genetics</topic><topic>Aquaporins</topic><topic>Aquaporins - chemistry</topic><topic>Atoms</topic><topic>Biological Sciences</topic><topic>Carbon Dioxide - chemistry</topic><topic>Cattle</topic><topic>Computational Biology - methods</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Glycerol - chemistry</topic><topic>Humans</topic><topic>Hydrogen bonds</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hydrophobicity</topic><topic>Lipid Bilayers - chemistry</topic><topic>Membranes</topic><topic>Molecular biology</topic><topic>Molecular interactions</topic><topic>Molecules</topic><topic>Oxygen - chemistry</topic><topic>Permeability</topic><topic>Point Mutation</topic><topic>Proteins</topic><topic>Signal Transduction - physiology</topic><topic>Solute movement</topic><topic>Solutes</topic><topic>Solutions</topic><topic>Studies</topic><topic>Thermodynamics</topic><topic>Umbrellas</topic><topic>Urea - chemistry</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hub, Jochen S</creatorcontrib><creatorcontrib>de Groot, Bert L</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hub, Jochen S</au><au>de Groot, Bert L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanism of selectivity in aquaporins and aquaglyceroporins</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2008-01-29</date><risdate>2008</risdate><volume>105</volume><issue>4</issue><spage>1198</spage><epage>1203</epage><pages>1198-1203</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Aquaporins and aquaglyceroporins form a family of pore proteins that facilitate the efficient and selective flux of small solutes across biological membranes. We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O₂, CO₂, NH₃, glycerol, urea, and water. Using molecular dynamics simulations, we calculated potentials of mean force for solute permeation along the aquaporin channels and compared them with the alternative pathway across the lipid bilayer. For small solutes permeating through AQP1, a remarkable anticorrelation between permeability and solute hydrophobicity was observed, whereas the opposite trend was observed for permeation through the membrane. This finding renders AQP1 a selective filter for small polar solutes, whereas GlpF was found to be highly permeable for small solutes and permeable for larger solutes. Surprisingly, not solute-channel but water-channel interactions were found to be the key determinant underlying the selectivity mechanism of aquaporins. Hence, a hydrophobic effect, together with steric restraints, determines the selectivity of aquaporins.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>18202181</pmid><doi>10.1073/pnas.0707662104</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Ammonia Ammonia - chemistry Animals Aquaglyceroporins Aquaglyceroporins - chemistry Aquaporin 1 - chemistry Aquaporin 1 - genetics Aquaporins Aquaporins - chemistry Atoms Biological Sciences Carbon Dioxide - chemistry Cattle Computational Biology - methods Escherichia coli Proteins - chemistry Glycerol - chemistry Humans Hydrogen bonds Hydrophobic and Hydrophilic Interactions Hydrophobicity Lipid Bilayers - chemistry Membranes Molecular biology Molecular interactions Molecules Oxygen - chemistry Permeability Point Mutation Proteins Signal Transduction - physiology Solute movement Solutes Solutions Studies Thermodynamics Umbrellas Urea - chemistry Water - chemistry |
| title | Mechanism of selectivity in aquaporins and aquaglyceroporins |
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