The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H +-ATPase subunit Vma7p
The phosphatidylinositol 3-kinase Vps34p of Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with C. albicans Vps34p and demonstrate physical interaction of Vps34p with...
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Veröffentlicht in: | International journal of medical microbiology 2005-04, Vol.295 (1), p.57-66 |
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creator | Eck, Raimund Nguyen, Monika Günther, Juliane Künkel, Waldemar Zipfel, Peter F. |
description | The phosphatidylinositol 3-kinase Vps34p of
Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with
C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H
+-ATPase Vma7p. The interaction initially observed in a yeast two-hybrid system was confirmed in vitro with recombinant proteins. Functional assays show that the Vps34p protein is necessary for vacuolar acidification and growth at alkaline pH. In addition, the
vps34 null mutant of
C. albicans shows defective autophagocytosis. The relevance of these functions for virulence of
C. albicans is discussed. |
doi_str_mv | 10.1016/j.ijmm.2004.12.007 |
format | Article |
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Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with
C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H
+-ATPase Vma7p. The interaction initially observed in a yeast two-hybrid system was confirmed in vitro with recombinant proteins. Functional assays show that the Vps34p protein is necessary for vacuolar acidification and growth at alkaline pH. In addition, the
vps34 null mutant of
C. albicans shows defective autophagocytosis. The relevance of these functions for virulence of
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Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with
C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H
+-ATPase Vma7p. The interaction initially observed in a yeast two-hybrid system was confirmed in vitro with recombinant proteins. Functional assays show that the Vps34p protein is necessary for vacuolar acidification and growth at alkaline pH. In addition, the
vps34 null mutant of
C. albicans shows defective autophagocytosis. The relevance of these functions for virulence of
C. albicans is discussed.</description><subject>Autophagy - physiology</subject><subject>Candida albicans</subject><subject>Candida albicans - enzymology</subject><subject>Candida albicans - metabolism</subject><subject>Gene Deletion</subject><subject>Genes, Fungal</subject><subject>Hydrogen-Ion Concentration</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>PtdIns 3-kinase</subject><subject>Two-Hybrid System Techniques</subject><subject>V-ATPase</subject><subject>Vacuolar Proton-Translocating ATPases - metabolism</subject><subject>Vacuoles - metabolism</subject><subject>Virulence</subject><subject>Vma7p</subject><subject>Vps34p</subject><issn>1438-4221</issn><issn>1618-0607</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUGL1DAYhoso7rr6BzxI8LAXaU3SbJoBL8ugrrCgh3GvIU2_2q-2SW2Skfll_j0zzoDgQXJIDs_38OZ7i-IloxWjTL4dKxznueKUiorxitLmUXHJJFMllbR5nN-iVqXgnF0Uz0IYKaV8U8unxQW7URljzWXxazcAWQYflsFE7A4TOh8w-onU5Xd0JgB5WEItFuJ7EjM7pNk4spg4-G_g0JIDmBDJ1rgOO0PM1KI1LhAMxJA5TRH75GxE78xEltVHQJdFJhJ0EVZjYyA_MQ5_5EuKOcUeyN7Y5CezkjvyprzdfTnmCKlNDiN5mE2zPC-e9GYK8OJ8XxVfP7zfbe_K-88fP21v70tbKxZL2WygUVwJywyXshWgpGBty63s2AY6YE0-ULeci77l7aaxrLVWKGW7G85sfVVcn7w5-o8EIeoZg4VpMg58Clo2Ku-digy-_gccfVrzp4PmVHDF65pmiJ8gu_oQVuj1suJs1oNmVB871aM-dqqPnWrGdXbnoVdnc2pn6P6OnEvMwLsTAHkRe4RVB4vgLHS4go268_g__28yU7WA</recordid><startdate>20050401</startdate><enddate>20050401</enddate><creator>Eck, Raimund</creator><creator>Nguyen, Monika</creator><creator>Günther, Juliane</creator><creator>Künkel, Waldemar</creator><creator>Zipfel, Peter F.</creator><general>Elsevier GmbH</general><general>Elsevier Science Ltd</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>K9.</scope><scope>7X8</scope></search><sort><creationdate>20050401</creationdate><title>The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H +-ATPase subunit Vma7p</title><author>Eck, Raimund ; Nguyen, Monika ; Günther, Juliane ; Künkel, Waldemar ; Zipfel, Peter F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-679e78284c1a266b4e8641bb2c6d19ede17171e3b224fb2b97c1bcc488cd521c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Autophagy - physiology</topic><topic>Candida albicans</topic><topic>Candida albicans - enzymology</topic><topic>Candida albicans - metabolism</topic><topic>Gene Deletion</topic><topic>Genes, Fungal</topic><topic>Hydrogen-Ion Concentration</topic><topic>Phosphatidylinositol 3-Kinases - genetics</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>PtdIns 3-kinase</topic><topic>Two-Hybrid System Techniques</topic><topic>V-ATPase</topic><topic>Vacuolar Proton-Translocating ATPases - metabolism</topic><topic>Vacuoles - metabolism</topic><topic>Virulence</topic><topic>Vma7p</topic><topic>Vps34p</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eck, Raimund</creatorcontrib><creatorcontrib>Nguyen, Monika</creatorcontrib><creatorcontrib>Günther, Juliane</creatorcontrib><creatorcontrib>Künkel, Waldemar</creatorcontrib><creatorcontrib>Zipfel, Peter F.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of medical microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eck, Raimund</au><au>Nguyen, Monika</au><au>Günther, Juliane</au><au>Künkel, Waldemar</au><au>Zipfel, Peter F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H +-ATPase subunit Vma7p</atitle><jtitle>International journal of medical microbiology</jtitle><addtitle>Int J Med Microbiol</addtitle><date>2005-04-01</date><risdate>2005</risdate><volume>295</volume><issue>1</issue><spage>57</spage><epage>66</epage><pages>57-66</pages><issn>1438-4221</issn><eissn>1618-0607</eissn><abstract>The phosphatidylinositol 3-kinase Vps34p of
Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with
C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H
+-ATPase Vma7p. The interaction initially observed in a yeast two-hybrid system was confirmed in vitro with recombinant proteins. Functional assays show that the Vps34p protein is necessary for vacuolar acidification and growth at alkaline pH. In addition, the
vps34 null mutant of
C. albicans shows defective autophagocytosis. The relevance of these functions for virulence of
C. albicans is discussed.</abstract><cop>Germany</cop><pub>Elsevier GmbH</pub><pmid>15861817</pmid><doi>10.1016/j.ijmm.2004.12.007</doi><tpages>10</tpages></addata></record> |
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source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Autophagy - physiology Candida albicans Candida albicans - enzymology Candida albicans - metabolism Gene Deletion Genes, Fungal Hydrogen-Ion Concentration Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - metabolism Protein Binding Protein Interaction Mapping PtdIns 3-kinase Two-Hybrid System Techniques V-ATPase Vacuolar Proton-Translocating ATPases - metabolism Vacuoles - metabolism Virulence Vma7p Vps34p |
title | The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H +-ATPase subunit Vma7p |
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