Functional Cooperativity of Enzymes of Phosphoinositide Conversion According to Synergistic Effects on Pectin Secretion in Tobacco Pollen Tubes
The Arabidopsis phosphoinositide kinases PI4Kβ1 and PIP5K5 have been implicated in the control of directional vesicle trafficking underlying polar tip growth in pollen tubes. PI4Kβ1 and PIP5K5 catalyze key consecutive steps of phosphoinositide conversion, and it appears obvious that phosphatidylinos...
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| Veröffentlicht in: | Molecular plant 2010-09, Vol.3 (5), p.870-881 |
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| creator | Ischebeck, Till Vu, Linh Hai Jin, Xu Stenzel, Irene Löfke, Christian Heilmann, Ingo |
| description | The Arabidopsis phosphoinositide kinases PI4Kβ1 and PIP5K5 have been implicated in the control of directional vesicle trafficking underlying polar tip growth in pollen tubes. PI4Kβ1 and PIP5K5 catalyze key consecutive steps of phosphoinositide conversion, and it appears obvious that phosphatidylinositol-4-phosphate formed by PI4Kβ1 might act as a substrate for phosphatidylinositol-4,5-bisphosphate formation by PIP5K5. However, this hypothesis has not been experimentally addressed and distinct localization patterns of PI4Kβ1, PIP5K5, and also PI-synthases （PIS） generating phosphatidylinositol suggest additional complexity. Here, the synergistic functionality of enzymes of phosphoinositide conversion was assessed. In tobacco and Arabidopsis pollen tubes, phosphoinositides influence the apical secretion of pectin, and increased pectin deposition results in characteristic morphological alterations. Catalytically active and dominant negative variants of PI4Kβ1 and PIP5K5 were systematically co-expressed in tobacco pollen tubes and the incidence of morphologies related to enhanced pectin secretion was evaluated. The data support a proposed functional interplay of PI4Kβ1 and PIP5K5 at the trans-Golgi network, mediating directional vesicle trafficking. Co-expression experiments additionally including PIS isoforms, PIS1 or PIS2, indicate that pectin secretion is synergistically mediated by PI4Kβ1 and PIPSK5 acting on Ptdlns formed by PIS2 rather than PIS1. Possible ramifications for the preferential channeling of phosphoinositide intermediates between particular isoforms of PI pathway enzymes are discussed. |
| doi_str_mv | 10.1093/mp/ssq031 |
| format | Article |
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PI4Kβ1 and PIP5K5 catalyze key consecutive steps of phosphoinositide conversion, and it appears obvious that phosphatidylinositol-4-phosphate formed by PI4Kβ1 might act as a substrate for phosphatidylinositol-4,5-bisphosphate formation by PIP5K5. However, this hypothesis has not been experimentally addressed and distinct localization patterns of PI4Kβ1, PIP5K5, and also PI-synthases （PIS） generating phosphatidylinositol suggest additional complexity. Here, the synergistic functionality of enzymes of phosphoinositide conversion was assessed. In tobacco and Arabidopsis pollen tubes, phosphoinositides influence the apical secretion of pectin, and increased pectin deposition results in characteristic morphological alterations. Catalytically active and dominant negative variants of PI4Kβ1 and PIP5K5 were systematically co-expressed in tobacco pollen tubes and the incidence of morphologies related to enhanced pectin secretion was evaluated. The data support a proposed functional interplay of PI4Kβ1 and PIP5K5 at the trans-Golgi network, mediating directional vesicle trafficking. Co-expression experiments additionally including PIS isoforms, PIS1 or PIS2, indicate that pectin secretion is synergistically mediated by PI4Kβ1 and PIPSK5 acting on Ptdlns formed by PIS2 rather than PIS1. Possible ramifications for the preferential channeling of phosphoinositide intermediates between particular isoforms of PI pathway enzymes are discussed.</description><identifier>ISSN: 1674-2052</identifier><identifier>EISSN: 1752-9867</identifier><identifier>DOI: 10.1093/mp/ssq031</identifier><identifier>PMID: 20603382</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>1-Phosphatidylinositol 4-Kinase - genetics ; 1-Phosphatidylinositol 4-Kinase - metabolism ; cooperativity ; Enzymes ; Mutagenesis, Site-Directed ; Nicotiana - enzymology ; Nicotiana - genetics ; Nicotiana - metabolism ; pectin secretion ; Pectins - metabolism ; phosphatidylinositol 4-kinase ; Phosphatidylinositol synthase ; phosphatidylinositol-4-phosphate 5-kinase ; Phosphatidylinositols - metabolism ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plants, Genetically Modified - enzymology ; Plants, Genetically Modified - genetics ; Plants, Genetically Modified - metabolism ; Pollen ; Pollen Tube - enzymology ; Pollen Tube - genetics ; Pollen Tube - metabolism ; pollen tubes ; Tobacco ; 分泌 ; 协同 ; 效应酶 ; 果胶 ; 烟草 ; 磷脂 ; 磷酸肌醇 ; 花粉管</subject><ispartof>Molecular plant, 2010-09, Vol.3 (5), p.870-881</ispartof><rights>2010 The Authors. All rights reserved.</rights><rights>The Author 2010. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-8e4ce3c169b338621397cfce18a0f11dceb7872a6c2e07e6cb7cbe65853c79043</citedby><cites>FETCH-LOGICAL-c484t-8e4ce3c169b338621397cfce18a0f11dceb7872a6c2e07e6cb7cbe65853c79043</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/90143B/90143B.jpg</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20603382$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ischebeck, Till</creatorcontrib><creatorcontrib>Vu, Linh Hai</creatorcontrib><creatorcontrib>Jin, Xu</creatorcontrib><creatorcontrib>Stenzel, Irene</creatorcontrib><creatorcontrib>Löfke, Christian</creatorcontrib><creatorcontrib>Heilmann, Ingo</creatorcontrib><title>Functional Cooperativity of Enzymes of Phosphoinositide Conversion According to Synergistic Effects on Pectin Secretion in Tobacco Pollen Tubes</title><title>Molecular plant</title><addtitle>Molecular Plant</addtitle><description>The Arabidopsis phosphoinositide kinases PI4Kβ1 and PIP5K5 have been implicated in the control of directional vesicle trafficking underlying polar tip growth in pollen tubes. PI4Kβ1 and PIP5K5 catalyze key consecutive steps of phosphoinositide conversion, and it appears obvious that phosphatidylinositol-4-phosphate formed by PI4Kβ1 might act as a substrate for phosphatidylinositol-4,5-bisphosphate formation by PIP5K5. However, this hypothesis has not been experimentally addressed and distinct localization patterns of PI4Kβ1, PIP5K5, and also PI-synthases （PIS） generating phosphatidylinositol suggest additional complexity. Here, the synergistic functionality of enzymes of phosphoinositide conversion was assessed. In tobacco and Arabidopsis pollen tubes, phosphoinositides influence the apical secretion of pectin, and increased pectin deposition results in characteristic morphological alterations. Catalytically active and dominant negative variants of PI4Kβ1 and PIP5K5 were systematically co-expressed in tobacco pollen tubes and the incidence of morphologies related to enhanced pectin secretion was evaluated. The data support a proposed functional interplay of PI4Kβ1 and PIP5K5 at the trans-Golgi network, mediating directional vesicle trafficking. Co-expression experiments additionally including PIS isoforms, PIS1 or PIS2, indicate that pectin secretion is synergistically mediated by PI4Kβ1 and PIPSK5 acting on Ptdlns formed by PIS2 rather than PIS1. Possible ramifications for the preferential channeling of phosphoinositide intermediates between particular isoforms of PI pathway enzymes are discussed.</description><subject>1-Phosphatidylinositol 4-Kinase - genetics</subject><subject>1-Phosphatidylinositol 4-Kinase - metabolism</subject><subject>cooperativity</subject><subject>Enzymes</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nicotiana - enzymology</subject><subject>Nicotiana - genetics</subject><subject>Nicotiana - metabolism</subject><subject>pectin secretion</subject><subject>Pectins - metabolism</subject><subject>phosphatidylinositol 4-kinase</subject><subject>Phosphatidylinositol synthase</subject><subject>phosphatidylinositol-4-phosphate 5-kinase</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plants, Genetically Modified - enzymology</subject><subject>Plants, Genetically Modified - genetics</subject><subject>Plants, Genetically Modified - metabolism</subject><subject>Pollen</subject><subject>Pollen Tube - enzymology</subject><subject>Pollen Tube - genetics</subject><subject>Pollen Tube - metabolism</subject><subject>pollen tubes</subject><subject>Tobacco</subject><subject>分泌</subject><subject>协同</subject><subject>效应酶</subject><subject>果胶</subject><subject>烟草</subject><subject>磷脂</subject><subject>磷酸肌醇</subject><subject>花粉管</subject><issn>1674-2052</issn><issn>1752-9867</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM-O0zAQhy0EYlfLHngBZMGJQ1j_SezkuKq6gLQSlXY5W8lk0hoSO7WdSuUleGVctXDi5Bnp-41nPkLecvaJs0beTfNdjHsm-QtyzXUliqZW-mWulS4LwSpxRW5jtB0TknOhWPmaXAmmmJS1uCa_HxYHyXrXjnTl_YyhTfZg05H6ga7dr-OE8VRudj7OO2-djzbZHjPsDhhiTtJ7AB9667Y0efp0dBi2NiYLdD0MCCnnHd3kwjr6hBDw9B3NzbPv2hylGz-OmNulw_iGvBraMeLt5b0h3x_Wz6svxeO3z19X948FlHWZihpLQAlcNV2-QwkuGw0DIK9bNnDeA3a61qJVIJBpVNBp6FBVdSVBN6yUN-TDee4c_H7BmMwPv4RsIRrOBGNNXbE6Ux_PFAQfY8DBzMFObThmyJzsm2k2Z_uZfXeZuHQT9v_Iv64zIM8A5rsOFoOJYNEB9jZkO6b39r9j319W2Hm33WfLJlv7OdgRjaxUWcpSyz-iTaDV</recordid><startdate>20100901</startdate><enddate>20100901</enddate><creator>Ischebeck, Till</creator><creator>Vu, Linh Hai</creator><creator>Jin, Xu</creator><creator>Stenzel, Irene</creator><creator>Löfke, Christian</creator><creator>Heilmann, Ingo</creator><general>Elsevier Inc</general><general>Cell Press</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>WU4</scope><scope>~WA</scope><scope>6I.</scope><scope>AAFTH</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>K9.</scope></search><sort><creationdate>20100901</creationdate><title>Functional Cooperativity of Enzymes of Phosphoinositide Conversion According to Synergistic Effects on Pectin Secretion in Tobacco Pollen Tubes</title><author>Ischebeck, Till ; Vu, Linh Hai ; Jin, Xu ; Stenzel, Irene ; Löfke, Christian ; Heilmann, Ingo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-8e4ce3c169b338621397cfce18a0f11dceb7872a6c2e07e6cb7cbe65853c79043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>1-Phosphatidylinositol 4-Kinase - genetics</topic><topic>1-Phosphatidylinositol 4-Kinase - metabolism</topic><topic>cooperativity</topic><topic>Enzymes</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nicotiana - enzymology</topic><topic>Nicotiana - genetics</topic><topic>Nicotiana - metabolism</topic><topic>pectin secretion</topic><topic>Pectins - metabolism</topic><topic>phosphatidylinositol 4-kinase</topic><topic>Phosphatidylinositol synthase</topic><topic>phosphatidylinositol-4-phosphate 5-kinase</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Plants, Genetically Modified - enzymology</topic><topic>Plants, Genetically Modified - genetics</topic><topic>Plants, Genetically Modified - metabolism</topic><topic>Pollen</topic><topic>Pollen Tube - enzymology</topic><topic>Pollen Tube - genetics</topic><topic>Pollen Tube - metabolism</topic><topic>pollen tubes</topic><topic>Tobacco</topic><topic>分泌</topic><topic>协同</topic><topic>效应酶</topic><topic>果胶</topic><topic>烟草</topic><topic>磷脂</topic><topic>磷酸肌醇</topic><topic>花粉管</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ischebeck, Till</creatorcontrib><creatorcontrib>Vu, Linh Hai</creatorcontrib><creatorcontrib>Jin, Xu</creatorcontrib><creatorcontrib>Stenzel, Irene</creatorcontrib><creatorcontrib>Löfke, Christian</creatorcontrib><creatorcontrib>Heilmann, Ingo</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库-自然科学</collection><collection>中文科技期刊数据库-自然科学-生物科学</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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 Health & Medical Complete (Alumni)</collection><jtitle>Molecular plant</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ischebeck, Till</au><au>Vu, Linh Hai</au><au>Jin, Xu</au><au>Stenzel, Irene</au><au>Löfke, Christian</au><au>Heilmann, Ingo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional Cooperativity of Enzymes of Phosphoinositide Conversion According to Synergistic Effects on Pectin Secretion in Tobacco Pollen Tubes</atitle><jtitle>Molecular plant</jtitle><addtitle>Molecular Plant</addtitle><date>2010-09-01</date><risdate>2010</risdate><volume>3</volume><issue>5</issue><spage>870</spage><epage>881</epage><pages>870-881</pages><issn>1674-2052</issn><eissn>1752-9867</eissn><abstract>The Arabidopsis phosphoinositide kinases PI4Kβ1 and PIP5K5 have been implicated in the control of directional vesicle trafficking underlying polar tip growth in pollen tubes. PI4Kβ1 and PIP5K5 catalyze key consecutive steps of phosphoinositide conversion, and it appears obvious that phosphatidylinositol-4-phosphate formed by PI4Kβ1 might act as a substrate for phosphatidylinositol-4,5-bisphosphate formation by PIP5K5. However, this hypothesis has not been experimentally addressed and distinct localization patterns of PI4Kβ1, PIP5K5, and also PI-synthases （PIS） generating phosphatidylinositol suggest additional complexity. Here, the synergistic functionality of enzymes of phosphoinositide conversion was assessed. In tobacco and Arabidopsis pollen tubes, phosphoinositides influence the apical secretion of pectin, and increased pectin deposition results in characteristic morphological alterations. Catalytically active and dominant negative variants of PI4Kβ1 and PIP5K5 were systematically co-expressed in tobacco pollen tubes and the incidence of morphologies related to enhanced pectin secretion was evaluated. The data support a proposed functional interplay of PI4Kβ1 and PIP5K5 at the trans-Golgi network, mediating directional vesicle trafficking. Co-expression experiments additionally including PIS isoforms, PIS1 or PIS2, indicate that pectin secretion is synergistically mediated by PI4Kβ1 and PIPSK5 acting on Ptdlns formed by PIS2 rather than PIS1. Possible ramifications for the preferential channeling of phosphoinositide intermediates between particular isoforms of PI pathway enzymes are discussed.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>20603382</pmid><doi>10.1093/mp/ssq031</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular plant, 2010-09, Vol.3 (5), p.870-881 |
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| subjects | 1-Phosphatidylinositol 4-Kinase - genetics 1-Phosphatidylinositol 4-Kinase - metabolism cooperativity Enzymes Mutagenesis, Site-Directed Nicotiana - enzymology Nicotiana - genetics Nicotiana - metabolism pectin secretion Pectins - metabolism phosphatidylinositol 4-kinase Phosphatidylinositol synthase phosphatidylinositol-4-phosphate 5-kinase Phosphatidylinositols - metabolism Plant Proteins - genetics Plant Proteins - metabolism Plants, Genetically Modified - enzymology Plants, Genetically Modified - genetics Plants, Genetically Modified - metabolism Pollen Pollen Tube - enzymology Pollen Tube - genetics Pollen Tube - metabolism pollen tubes Tobacco 分泌 协同 效应酶 果胶 烟草 磷脂 磷酸肌醇 花粉管 |
| title | Functional Cooperativity of Enzymes of Phosphoinositide Conversion According to Synergistic Effects on Pectin Secretion in Tobacco Pollen Tubes |
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