SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34
Salmonella colonizes a vacuolar niche in host cells during infection. Maturation of the Salmonella-containing vacuole (SCV) involves the formation of phosphatidylinositol 3-phosphate (PI(3)P) on its outer leaflet. SopB, a bacterial virulence factor with phosphoinositide phosphatase activity, was pro...
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| Veröffentlicht in: | The Journal of cell biology 2008-08, Vol.182 (4), p.741-752 |
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| container_title | The Journal of cell biology |
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| creator | Mallo, Gustavo V Espina, Marianela Smith, Adam C Terebiznik, Mauricio R Alemán, Ainel Finlay, B. Brett Rameh, Lucia E Grinstein, Sergio Brumell, John H |
| description | Salmonella colonizes a vacuolar niche in host cells during infection. Maturation of the Salmonella-containing vacuole (SCV) involves the formation of phosphatidylinositol 3-phosphate (PI(3)P) on its outer leaflet. SopB, a bacterial virulence factor with phosphoinositide phosphatase activity, was proposed to generate PI(3)P by dephosphorylating PI(3,4)P2, PI(3,5)P2, and PI(3,4,5)P3. Here, we examine the mechanism of PI(3)P formation during Salmonella infection. SopB is required to form PI(3,4)P2/PI(3,4,5)P3 at invasion ruffles and PI(3)P on nascent SCVs. However, we uncouple these events experimentally and reveal that SopB does not dephosphorylate PI(3,4)P2/PI(3,4,5)P3 to produce PI(3)P. Instead, the phosphatase activity of SopB is required for Rab5 recruitment to the SCV. Vps34, a PI3-kinase that associates with active Rab5, is responsible for PI(3)P formation on SCVs. Therefore, SopB mediates PI(3)P production on the SCV indirectly through recruitment of Rab5 and its effector Vps34. These findings reveal a link between phosphoinositide phosphatase activity and the recruitment of Rab5 to phagosomes. |
| doi_str_mv | 10.1083/jcb.200804131 |
| format | Article |
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Brett ; Rameh, Lucia E ; Grinstein, Sergio ; Brumell, John H</creator><creatorcontrib>Mallo, Gustavo V ; Espina, Marianela ; Smith, Adam C ; Terebiznik, Mauricio R ; Alemán, Ainel ; Finlay, B. Brett ; Rameh, Lucia E ; Grinstein, Sergio ; Brumell, John H</creatorcontrib><description>Salmonella colonizes a vacuolar niche in host cells during infection. Maturation of the Salmonella-containing vacuole (SCV) involves the formation of phosphatidylinositol 3-phosphate (PI(3)P) on its outer leaflet. SopB, a bacterial virulence factor with phosphoinositide phosphatase activity, was proposed to generate PI(3)P by dephosphorylating PI(3,4)P2, PI(3,5)P2, and PI(3,4,5)P3. Here, we examine the mechanism of PI(3)P formation during Salmonella infection. SopB is required to form PI(3,4)P2/PI(3,4,5)P3 at invasion ruffles and PI(3)P on nascent SCVs. However, we uncouple these events experimentally and reveal that SopB does not dephosphorylate PI(3,4)P2/PI(3,4,5)P3 to produce PI(3)P. Instead, the phosphatase activity of SopB is required for Rab5 recruitment to the SCV. Vps34, a PI3-kinase that associates with active Rab5, is responsible for PI(3)P formation on SCVs. Therefore, SopB mediates PI(3)P production on the SCV indirectly through recruitment of Rab5 and its effector Vps34. These findings reveal a link between phosphoinositide phosphatase activity and the recruitment of Rab5 to phagosomes.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200804131</identifier><identifier>PMID: 18725540</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Bacteria ; Bacterial Proteins - metabolism ; Bacteriology ; Biological Transport - drug effects ; Cell Membrane - drug effects ; Cell Membrane - enzymology ; Cell membranes ; Cell Surface Extensions - drug effects ; Cellular biology ; Enzyme Activation - drug effects ; HeLa Cells ; Humans ; Infections ; Kinases ; Lipids ; Models, Biological ; Mutation - genetics ; Phosphatases ; Phosphates ; Phosphatidylinositol 3-Kinases - antagonists & inhibitors ; Phosphatidylinositol 3-Kinases - metabolism ; Phosphatidylinositol Phosphates - metabolism ; Phosphatidylinositols ; Protein Kinase Inhibitors - pharmacology ; rab5 GTP-Binding Proteins - metabolism ; Ruffles ; Salmonella ; Salmonella - cytology ; Salmonella - drug effects ; Salmonella - enzymology ; Small interfering RNA ; Vacuoles ; Vacuoles - drug effects ; Vacuoles - enzymology</subject><ispartof>The Journal of cell biology, 2008-08, Vol.182 (4), p.741-752</ispartof><rights>Copyright Rockefeller University Press Aug 25, 2008</rights><rights>2008 Mallo et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-6287968186d612adcd9e4c9db98187350d5c8bedec74106d7cbbbf302c76c6043</citedby><cites>FETCH-LOGICAL-c524t-6287968186d612adcd9e4c9db98187350d5c8bedec74106d7cbbbf302c76c6043</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,777,781,882,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18725540$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mallo, Gustavo V</creatorcontrib><creatorcontrib>Espina, Marianela</creatorcontrib><creatorcontrib>Smith, Adam C</creatorcontrib><creatorcontrib>Terebiznik, Mauricio R</creatorcontrib><creatorcontrib>Alemán, Ainel</creatorcontrib><creatorcontrib>Finlay, B. Brett</creatorcontrib><creatorcontrib>Rameh, Lucia E</creatorcontrib><creatorcontrib>Grinstein, Sergio</creatorcontrib><creatorcontrib>Brumell, John H</creatorcontrib><title>SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Salmonella colonizes a vacuolar niche in host cells during infection. Maturation of the Salmonella-containing vacuole (SCV) involves the formation of phosphatidylinositol 3-phosphate (PI(3)P) on its outer leaflet. SopB, a bacterial virulence factor with phosphoinositide phosphatase activity, was proposed to generate PI(3)P by dephosphorylating PI(3,4)P2, PI(3,5)P2, and PI(3,4,5)P3. Here, we examine the mechanism of PI(3)P formation during Salmonella infection. SopB is required to form PI(3,4)P2/PI(3,4,5)P3 at invasion ruffles and PI(3)P on nascent SCVs. However, we uncouple these events experimentally and reveal that SopB does not dephosphorylate PI(3,4)P2/PI(3,4,5)P3 to produce PI(3)P. Instead, the phosphatase activity of SopB is required for Rab5 recruitment to the SCV. Vps34, a PI3-kinase that associates with active Rab5, is responsible for PI(3)P formation on SCVs. Therefore, SopB mediates PI(3)P production on the SCV indirectly through recruitment of Rab5 and its effector Vps34. These findings reveal a link between phosphoinositide phosphatase activity and the recruitment of Rab5 to phagosomes.</description><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological Transport - drug effects</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - enzymology</subject><subject>Cell membranes</subject><subject>Cell Surface Extensions - drug effects</subject><subject>Cellular biology</subject><subject>Enzyme Activation - drug effects</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Infections</subject><subject>Kinases</subject><subject>Lipids</subject><subject>Models, Biological</subject><subject>Mutation - genetics</subject><subject>Phosphatases</subject><subject>Phosphates</subject><subject>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Phosphatidylinositol Phosphates - metabolism</subject><subject>Phosphatidylinositols</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>rab5 GTP-Binding Proteins - metabolism</subject><subject>Ruffles</subject><subject>Salmonella</subject><subject>Salmonella - cytology</subject><subject>Salmonella - drug effects</subject><subject>Salmonella - enzymology</subject><subject>Small interfering RNA</subject><subject>Vacuoles</subject><subject>Vacuoles - drug effects</subject><subject>Vacuoles - enzymology</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUuLFDEURoMoTs_o0qUaZuGuxptnVW0EHXzBgGA7bkMqSXWnSVVqkqqB_vdm6LZ9QCCQ7_DlXg5CLwhcEWjY253prihAA5ww8gitiOBQNYTDY7QCoKRqBRVn6DznHQDwmrOn6Iw0NRUFXKGwjtMHPKU4xNllPG1jnrZ69nYf_Bizn2PArPr97HAf01DiOOJy1joMcXQhaHyvzRJDaej2ODmTFj_7cYO_605gPVr8c8qMP0NPeh2ye368L9Dtp48_rr9UN98-f71-f1MZQflcSdrUrWxII60kVFtjW8dNa7u2vNVMgBWm6Zx1puYEpK1N13U9A2pqaSRwdoHeHXqnpRucNW6ckw5qSn7Qaa-i9urfZPRbtYn3ioryAaGl4M2xIMW7xeVZDT6bh0VHF5esZMulEIIV8PI_cBeXNJblFCV1EVRLKFB1gEyKOSfXnyYhoB4kqiJRnSQW_tXf4_-hj9YK8PIA7PIc0ymnRa-Etin560Pe66j0JvmsbtcUCANoGQgh2S9cjaxf</recordid><startdate>20080825</startdate><enddate>20080825</enddate><creator>Mallo, Gustavo V</creator><creator>Espina, Marianela</creator><creator>Smith, Adam C</creator><creator>Terebiznik, Mauricio R</creator><creator>Alemán, Ainel</creator><creator>Finlay, B. Brett</creator><creator>Rameh, Lucia E</creator><creator>Grinstein, Sergio</creator><creator>Brumell, John H</creator><general>The Rockefeller University Press</general><general>Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>20080825</creationdate><title>SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34</title><author>Mallo, Gustavo V ; Espina, Marianela ; Smith, Adam C ; Terebiznik, Mauricio R ; Alemán, Ainel ; Finlay, B. Brett ; Rameh, Lucia E ; Grinstein, Sergio ; Brumell, John H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c524t-6287968186d612adcd9e4c9db98187350d5c8bedec74106d7cbbbf302c76c6043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Bacteria</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological Transport - drug effects</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - enzymology</topic><topic>Cell membranes</topic><topic>Cell Surface Extensions - drug effects</topic><topic>Cellular biology</topic><topic>Enzyme Activation - drug effects</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Infections</topic><topic>Kinases</topic><topic>Lipids</topic><topic>Models, Biological</topic><topic>Mutation - genetics</topic><topic>Phosphatases</topic><topic>Phosphates</topic><topic>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Phosphatidylinositol Phosphates - metabolism</topic><topic>Phosphatidylinositols</topic><topic>Protein Kinase Inhibitors - pharmacology</topic><topic>rab5 GTP-Binding Proteins - metabolism</topic><topic>Ruffles</topic><topic>Salmonella</topic><topic>Salmonella - cytology</topic><topic>Salmonella - drug effects</topic><topic>Salmonella - enzymology</topic><topic>Small interfering RNA</topic><topic>Vacuoles</topic><topic>Vacuoles - drug effects</topic><topic>Vacuoles - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mallo, Gustavo V</creatorcontrib><creatorcontrib>Espina, Marianela</creatorcontrib><creatorcontrib>Smith, Adam C</creatorcontrib><creatorcontrib>Terebiznik, Mauricio R</creatorcontrib><creatorcontrib>Alemán, Ainel</creatorcontrib><creatorcontrib>Finlay, B. Brett</creatorcontrib><creatorcontrib>Rameh, Lucia E</creatorcontrib><creatorcontrib>Grinstein, Sergio</creatorcontrib><creatorcontrib>Brumell, John H</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mallo, Gustavo V</au><au>Espina, Marianela</au><au>Smith, Adam C</au><au>Terebiznik, Mauricio R</au><au>Alemán, Ainel</au><au>Finlay, B. Brett</au><au>Rameh, Lucia E</au><au>Grinstein, Sergio</au><au>Brumell, John H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2008-08-25</date><risdate>2008</risdate><volume>182</volume><issue>4</issue><spage>741</spage><epage>752</epage><pages>741-752</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Salmonella colonizes a vacuolar niche in host cells during infection. Maturation of the Salmonella-containing vacuole (SCV) involves the formation of phosphatidylinositol 3-phosphate (PI(3)P) on its outer leaflet. SopB, a bacterial virulence factor with phosphoinositide phosphatase activity, was proposed to generate PI(3)P by dephosphorylating PI(3,4)P2, PI(3,5)P2, and PI(3,4,5)P3. Here, we examine the mechanism of PI(3)P formation during Salmonella infection. SopB is required to form PI(3,4)P2/PI(3,4,5)P3 at invasion ruffles and PI(3)P on nascent SCVs. However, we uncouple these events experimentally and reveal that SopB does not dephosphorylate PI(3,4)P2/PI(3,4,5)P3 to produce PI(3)P. Instead, the phosphatase activity of SopB is required for Rab5 recruitment to the SCV. Vps34, a PI3-kinase that associates with active Rab5, is responsible for PI(3)P formation on SCVs. Therefore, SopB mediates PI(3)P production on the SCV indirectly through recruitment of Rab5 and its effector Vps34. These findings reveal a link between phosphoinositide phosphatase activity and the recruitment of Rab5 to phagosomes.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>18725540</pmid><doi>10.1083/jcb.200804131</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacteria Bacterial Proteins - metabolism Bacteriology Biological Transport - drug effects Cell Membrane - drug effects Cell Membrane - enzymology Cell membranes Cell Surface Extensions - drug effects Cellular biology Enzyme Activation - drug effects HeLa Cells Humans Infections Kinases Lipids Models, Biological Mutation - genetics Phosphatases Phosphates Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - metabolism Phosphatidylinositol Phosphates - metabolism Phosphatidylinositols Protein Kinase Inhibitors - pharmacology rab5 GTP-Binding Proteins - metabolism Ruffles Salmonella Salmonella - cytology Salmonella - drug effects Salmonella - enzymology Small interfering RNA Vacuoles Vacuoles - drug effects Vacuoles - enzymology |
| title | SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34 |
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