Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER
Abstract Cholera toxin (CT), and members of the AB5 family of toxins enter host cells and hijack the cell's endogenous pathways to induce toxicity. CT binds to a lipid receptor on the plasma membrane (PM), ganglioside GM1, which has the ability to associate with lipid rafts. The toxin can then...
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creator | Chinnapen, Daniel J.-F. Chinnapen, Himani Saslowsky, David Lencer, Wayne I. |
description | Abstract
Cholera toxin (CT), and members of the AB5 family of toxins enter host cells and hijack the cell's endogenous pathways to induce toxicity. CT binds to a lipid receptor on the plasma membrane (PM), ganglioside GM1, which has the ability to associate with lipid rafts. The toxin can then enter the cell by various modes of receptor-mediated endocytosis and traffic in a retrograde manner from the PM to the Golgi and the endoplasmic reticulum (ER). Once in the ER, a portion of the toxin is unfolded and retro-translocated to the cytosol so as to induce disease. GM1 is the vehicle that carries CT from PM to ER. Thus, the toxin pathway from PM to ER is a lipid-based sorting pathway, which is potentially meditated by the determinants of the GM1 ganglioside structure itself. |
doi_str_mv | 10.1111/j.1574-6968.2006.00545.x |
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Cholera toxin (CT), and members of the AB5 family of toxins enter host cells and hijack the cell's endogenous pathways to induce toxicity. CT binds to a lipid receptor on the plasma membrane (PM), ganglioside GM1, which has the ability to associate with lipid rafts. The toxin can then enter the cell by various modes of receptor-mediated endocytosis and traffic in a retrograde manner from the PM to the Golgi and the endoplasmic reticulum (ER). Once in the ER, a portion of the toxin is unfolded and retro-translocated to the cytosol so as to induce disease. GM1 is the vehicle that carries CT from PM to ER. Thus, the toxin pathway from PM to ER is a lipid-based sorting pathway, which is potentially meditated by the determinants of the GM1 ganglioside structure itself.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2006.00545.x</identifier><identifier>PMID: 17156122</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>AB5 toxin ; Animals ; Bacteriology ; Biological and medical sciences ; Cell Membrane - metabolism ; Cholera ; Cholera toxin ; Cholera Toxin - metabolism ; Cytosol ; Endocytosis ; Endocytosis - physiology ; Endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; Fundamental and applied biological sciences. Psychology ; Ganglioside GM1 ; GM1 ; Golgi apparatus ; Humans ; lipid raft ; Lipid rafts ; Lipids ; Membrane trafficking ; Membranes ; Microbiology ; Models, Biological ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Protein transport ; Protein Transport - physiology ; retrograde pathway ; Toxicity ; Toxins ; Waterborne diseases</subject><ispartof>FEMS microbiology letters, 2007-01, Vol.266 (2), p.129-137</ispartof><rights>2006 Federation of European Microbiological Societies 2006</rights><rights>2007 INIST-CNRS</rights><rights>2006 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5495-832d21bd0c1aa574233cf22339de61c9a1c9775b8707a3131a900b1eb07b98723</citedby><cites>FETCH-LOGICAL-c5495-832d21bd0c1aa574233cf22339de61c9a1c9775b8707a3131a900b1eb07b98723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2006.00545.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2006.00545.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,4022,27922,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18517721$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17156122$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chinnapen, Daniel J.-F.</creatorcontrib><creatorcontrib>Chinnapen, Himani</creatorcontrib><creatorcontrib>Saslowsky, David</creatorcontrib><creatorcontrib>Lencer, Wayne I.</creatorcontrib><title>Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Cholera toxin (CT), and members of the AB5 family of toxins enter host cells and hijack the cell's endogenous pathways to induce toxicity. CT binds to a lipid receptor on the plasma membrane (PM), ganglioside GM1, which has the ability to associate with lipid rafts. The toxin can then enter the cell by various modes of receptor-mediated endocytosis and traffic in a retrograde manner from the PM to the Golgi and the endoplasmic reticulum (ER). Once in the ER, a portion of the toxin is unfolded and retro-translocated to the cytosol so as to induce disease. GM1 is the vehicle that carries CT from PM to ER. Thus, the toxin pathway from PM to ER is a lipid-based sorting pathway, which is potentially meditated by the determinants of the GM1 ganglioside structure itself.</description><subject>AB5 toxin</subject><subject>Animals</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Cholera</subject><subject>Cholera toxin</subject><subject>Cholera Toxin - metabolism</subject><subject>Cytosol</subject><subject>Endocytosis</subject><subject>Endocytosis - physiology</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Ganglioside GM1</subject><subject>GM1</subject><subject>Golgi apparatus</subject><subject>Humans</subject><subject>lipid raft</subject><subject>Lipid rafts</subject><subject>Lipids</subject><subject>Membrane trafficking</subject><subject>Membranes</subject><subject>Microbiology</subject><subject>Models, Biological</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Protein transport</subject><subject>Protein Transport - physiology</subject><subject>retrograde pathway</subject><subject>Toxicity</subject><subject>Toxins</subject><subject>Waterborne diseases</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkO9r3CAch2WsrLd2_0IRyvou2VeNMZa9KaXdBlcKR_dajDGrtyTeNKF3__1M72hhYzDBH-Dz0Q8PQphATtL4tM4JF0VWyrLKKUCZA_CC59s3aPFy8RYtgIkqIyDFMXof4xoACgrlO3RMBOEloXSBVivdjm74gZ_c-IjNo-9s0Hj0WzdcYjs03uxGH13EemjwGHTbOvNz5tvge7zpdOw17m1fBz3YlMM3q1N01Oou2g-H_QR9v715uP6aLe-_fLu-WmaGF5JnFaMNJXUDhmidSlPGTEvTKhtbEiN1mkLwuhIgNCOMaAlQE1uDqGUlKDtBF_t3N8H_mmwcVe-isV2XmvgpKiJ5yapCJvD8D3DtpzCkbooyKDmjnIhEVXvKBB9jsK3aBNfrsFME1GxdrdUsV81y1WxdPVtX2xQ9O3ww1b1tXoMHzQn4eAB0NLprkyzj4itXpQKCksR93nNPrrO7_y6gbu-W6ZDibB_30-Yf4ezv9r8BMUyqTg</recordid><startdate>20070101</startdate><enddate>20070101</enddate><creator>Chinnapen, Daniel J.-F.</creator><creator>Chinnapen, Himani</creator><creator>Saslowsky, David</creator><creator>Lencer, Wayne I.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>IQODW</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7U7</scope></search><sort><creationdate>20070101</creationdate><title>Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER</title><author>Chinnapen, Daniel J.-F. ; Chinnapen, Himani ; Saslowsky, David ; Lencer, Wayne I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5495-832d21bd0c1aa574233cf22339de61c9a1c9775b8707a3131a900b1eb07b98723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>AB5 toxin</topic><topic>Animals</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Cholera</topic><topic>Cholera toxin</topic><topic>Cholera Toxin - metabolism</topic><topic>Cytosol</topic><topic>Endocytosis</topic><topic>Endocytosis - physiology</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Ganglioside GM1</topic><topic>GM1</topic><topic>Golgi apparatus</topic><topic>Humans</topic><topic>lipid raft</topic><topic>Lipid rafts</topic><topic>Lipids</topic><topic>Membrane trafficking</topic><topic>Membranes</topic><topic>Microbiology</topic><topic>Models, Biological</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Protein transport</topic><topic>Protein Transport - physiology</topic><topic>retrograde pathway</topic><topic>Toxicity</topic><topic>Toxins</topic><topic>Waterborne diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chinnapen, Daniel J.-F.</creatorcontrib><creatorcontrib>Chinnapen, Himani</creatorcontrib><creatorcontrib>Saslowsky, David</creatorcontrib><creatorcontrib>Lencer, Wayne I.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>Toxicology Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chinnapen, Daniel J.-F.</au><au>Chinnapen, Himani</au><au>Saslowsky, David</au><au>Lencer, Wayne I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2007-01-01</date><risdate>2007</risdate><volume>266</volume><issue>2</issue><spage>129</spage><epage>137</epage><pages>129-137</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
Cholera toxin (CT), and members of the AB5 family of toxins enter host cells and hijack the cell's endogenous pathways to induce toxicity. CT binds to a lipid receptor on the plasma membrane (PM), ganglioside GM1, which has the ability to associate with lipid rafts. The toxin can then enter the cell by various modes of receptor-mediated endocytosis and traffic in a retrograde manner from the PM to the Golgi and the endoplasmic reticulum (ER). Once in the ER, a portion of the toxin is unfolded and retro-translocated to the cytosol so as to induce disease. GM1 is the vehicle that carries CT from PM to ER. Thus, the toxin pathway from PM to ER is a lipid-based sorting pathway, which is potentially meditated by the determinants of the GM1 ganglioside structure itself.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>17156122</pmid><doi>10.1111/j.1574-6968.2006.00545.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); Wiley Online Library All Journals |
subjects | AB5 toxin Animals Bacteriology Biological and medical sciences Cell Membrane - metabolism Cholera Cholera toxin Cholera Toxin - metabolism Cytosol Endocytosis Endocytosis - physiology Endoplasmic reticulum Endoplasmic Reticulum - metabolism Fundamental and applied biological sciences. Psychology Ganglioside GM1 GM1 Golgi apparatus Humans lipid raft Lipid rafts Lipids Membrane trafficking Membranes Microbiology Models, Biological Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Protein transport Protein Transport - physiology retrograde pathway Toxicity Toxins Waterborne diseases |
title | Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER |
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