Enhancement of phosphoinositide 3‐kinase (PI 3‐kinase) activity by membrane curvature and inositol‐phospholipid‐binding peptides
The phosphorylation of phosphatidylinositol (PtdIns) on the 3′ position of the inositol ring by phosphoinositide 3‐kinase (PI 3‐kinase) is shown to depend strongly on the curvature of liposomes containing a mixture of phosphatidylcholine (PtdCho) and PtdIns. Vesicles with an average diameter of 50 n...
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| Veröffentlicht in: | European journal of biochemistry 1998-12, Vol.258 (2), p.846-853 |
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| container_title | European journal of biochemistry |
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| creator | Hübner, Stefan Couvillon, Anthony D. Käs, Josef A. Bankaitis, Vytas A. Vegners, Rolands Carpenter, Christopher L. Janmey, Paul A. |
| description | The phosphorylation of phosphatidylinositol (PtdIns) on the 3′ position of the inositol ring by phosphoinositide 3‐kinase (PI 3‐kinase) is shown to depend strongly on the curvature of liposomes containing a mixture of phosphatidylcholine (PtdCho) and PtdIns. Vesicles with an average diameter of 50 nm are phosphorylated 100 times faster than chemically identical vesicles with an average diameter greater than 300 nm. The low reactivity of large vesicles is not due to the difference in vesicle number for large and small vesicles at constant total lipid, nor to occlusion of lipid surfaces in multilammelar structures, and can be reversed by addition of low ( |
| doi_str_mv | 10.1046/j.1432-1327.1998.2580846.x |
| format | Article |
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Vesicles with an average diameter of 50 nm are phosphorylated 100 times faster than chemically identical vesicles with an average diameter greater than 300 nm. The low reactivity of large vesicles is not due to the difference in vesicle number for large and small vesicles at constant total lipid, nor to occlusion of lipid surfaces in multilammelar structures, and can be reversed by addition of low (< 1 : 100) molar ratios of either the PtdIns transfer protein sec14p or a ten‐residue peptide derived from the inositol‐phospholipid‐binding site of gelsolin. Similar measurements using PI 4‐kinase showed a weak dependence on vesicle size. The strong dependence of PI 3‐kinase function on membrane curvature suggests possible localization of PI 3‐kinase activity at sites where clustering of receptors, for example, may locally deform the membrane, and suggests that once PI 3‐kinase is localized and activated at surface sites, the reaction may become self‐accelerating.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1046/j.1432-1327.1998.2580846.x</identifier><identifier>PMID: 9874255</identifier><language>eng</language><publisher>Berlin & Heidelberg: Springer‐Verlag</publisher><subject>1-Phosphatidylinositol 4-Kinase - metabolism ; Adenosine Triphosphate - metabolism ; Animals ; Carrier Proteins - metabolism ; curvature ; Drug Compounding ; Enzyme Activation ; Fluorescent Dyes - metabolism ; gelsolin ; Gelsolin - chemistry ; inositolphospholipid ; Lipid Bilayers - metabolism ; Liposomes - metabolism ; Liver - enzymology ; Membrane Proteins ; Particle Size ; Peptide Fragments - metabolism ; Peptides - pharmacology ; phosphatidylinositol ; Phosphatidylinositol 3-Kinases - metabolism ; Phosphatidylinositols - metabolism ; Phospholipid Transfer Proteins ; PI 3‐kinase ; Rats ; Surface Properties</subject><ispartof>European journal of biochemistry, 1998-12, Vol.258 (2), p.846-853</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3746-8d4692fcfc0f4c26f3d3696e343535b36c880dd19011d851ec0ee228a33b49683</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1432-1327.1998.2580846.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1432-1327.1998.2580846.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9874255$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hübner, Stefan</creatorcontrib><creatorcontrib>Couvillon, Anthony D.</creatorcontrib><creatorcontrib>Käs, Josef A.</creatorcontrib><creatorcontrib>Bankaitis, Vytas A.</creatorcontrib><creatorcontrib>Vegners, Rolands</creatorcontrib><creatorcontrib>Carpenter, Christopher L.</creatorcontrib><creatorcontrib>Janmey, Paul A.</creatorcontrib><title>Enhancement of phosphoinositide 3‐kinase (PI 3‐kinase) activity by membrane curvature and inositol‐phospholipid‐binding peptides</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The phosphorylation of phosphatidylinositol (PtdIns) on the 3′ position of the inositol ring by phosphoinositide 3‐kinase (PI 3‐kinase) is shown to depend strongly on the curvature of liposomes containing a mixture of phosphatidylcholine (PtdCho) and PtdIns. Vesicles with an average diameter of 50 nm are phosphorylated 100 times faster than chemically identical vesicles with an average diameter greater than 300 nm. The low reactivity of large vesicles is not due to the difference in vesicle number for large and small vesicles at constant total lipid, nor to occlusion of lipid surfaces in multilammelar structures, and can be reversed by addition of low (< 1 : 100) molar ratios of either the PtdIns transfer protein sec14p or a ten‐residue peptide derived from the inositol‐phospholipid‐binding site of gelsolin. Similar measurements using PI 4‐kinase showed a weak dependence on vesicle size. The strong dependence of PI 3‐kinase function on membrane curvature suggests possible localization of PI 3‐kinase activity at sites where clustering of receptors, for example, may locally deform the membrane, and suggests that once PI 3‐kinase is localized and activated at surface sites, the reaction may become self‐accelerating.</description><subject>1-Phosphatidylinositol 4-Kinase - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Carrier Proteins - metabolism</subject><subject>curvature</subject><subject>Drug Compounding</subject><subject>Enzyme Activation</subject><subject>Fluorescent Dyes - metabolism</subject><subject>gelsolin</subject><subject>Gelsolin - chemistry</subject><subject>inositolphospholipid</subject><subject>Lipid Bilayers - metabolism</subject><subject>Liposomes - metabolism</subject><subject>Liver - enzymology</subject><subject>Membrane Proteins</subject><subject>Particle Size</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptides - pharmacology</subject><subject>phosphatidylinositol</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Phospholipid Transfer Proteins</subject><subject>PI 3‐kinase</subject><subject>Rats</subject><subject>Surface Properties</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVUcuO1DAQtBBoGRY-AcnigOCQ4FccmxuMZmGllUACzpZjd1gPiRPiZNm5ceTIN_IlJCRCXDm0WqXqqra7EHpCSU6JkC-OORWcZZSzMqdaq5wViigh89s7aLdShPO7aEcIFRnThbyPHqR0JIRILcszdKZVKVhR7NCPQ7y20UELccRdjfvrLs0VYpfCGDxg_uv7zy8h2gT42fvLf-BzbN0YbsJ4wtUJt9BWg42A3TTc2HEaANvo8erTNbNqc25CH_wMqxB9iJ9xD_2yJz1E92rbJHi09XP06eLwcf82u3r35nL_6ipzvBQyU15IzWpXO1ILx2TNPZ__BFzwghcVl04p4j3VhFKvCgqOADCmLOeV0FLxc_R09e2H7usEaTRtSA6aZn58NyUjNaW8_DP4ch10Q5fSALXph9Da4WQoMUsM5miWW5slBrPEYLYYzO0sfrxtmaoW_F_pdveZ36_8t9DA6T-czcXh9YcN8d-nKp37</recordid><startdate>199812</startdate><enddate>199812</enddate><creator>Hübner, Stefan</creator><creator>Couvillon, Anthony D.</creator><creator>Käs, Josef A.</creator><creator>Bankaitis, Vytas A.</creator><creator>Vegners, Rolands</creator><creator>Carpenter, Christopher L.</creator><creator>Janmey, Paul A.</creator><general>Springer‐Verlag</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>7X8</scope></search><sort><creationdate>199812</creationdate><title>Enhancement of phosphoinositide 3‐kinase (PI 3‐kinase) activity by membrane curvature and inositol‐phospholipid‐binding peptides</title><author>Hübner, Stefan ; Couvillon, Anthony D. ; Käs, Josef A. ; Bankaitis, Vytas A. ; Vegners, Rolands ; Carpenter, Christopher L. ; Janmey, Paul A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3746-8d4692fcfc0f4c26f3d3696e343535b36c880dd19011d851ec0ee228a33b49683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>1-Phosphatidylinositol 4-Kinase - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Carrier Proteins - metabolism</topic><topic>curvature</topic><topic>Drug Compounding</topic><topic>Enzyme Activation</topic><topic>Fluorescent Dyes - metabolism</topic><topic>gelsolin</topic><topic>Gelsolin - chemistry</topic><topic>inositolphospholipid</topic><topic>Lipid Bilayers - metabolism</topic><topic>Liposomes - metabolism</topic><topic>Liver - enzymology</topic><topic>Membrane Proteins</topic><topic>Particle Size</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptides - pharmacology</topic><topic>phosphatidylinositol</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Phospholipid Transfer Proteins</topic><topic>PI 3‐kinase</topic><topic>Rats</topic><topic>Surface Properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hübner, Stefan</creatorcontrib><creatorcontrib>Couvillon, Anthony D.</creatorcontrib><creatorcontrib>Käs, Josef A.</creatorcontrib><creatorcontrib>Bankaitis, Vytas A.</creatorcontrib><creatorcontrib>Vegners, Rolands</creatorcontrib><creatorcontrib>Carpenter, Christopher L.</creatorcontrib><creatorcontrib>Janmey, Paul A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hübner, Stefan</au><au>Couvillon, Anthony D.</au><au>Käs, Josef A.</au><au>Bankaitis, Vytas A.</au><au>Vegners, Rolands</au><au>Carpenter, Christopher L.</au><au>Janmey, Paul A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhancement of phosphoinositide 3‐kinase (PI 3‐kinase) activity by membrane curvature and inositol‐phospholipid‐binding peptides</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1998-12</date><risdate>1998</risdate><volume>258</volume><issue>2</issue><spage>846</spage><epage>853</epage><pages>846-853</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The phosphorylation of phosphatidylinositol (PtdIns) on the 3′ position of the inositol ring by phosphoinositide 3‐kinase (PI 3‐kinase) is shown to depend strongly on the curvature of liposomes containing a mixture of phosphatidylcholine (PtdCho) and PtdIns. Vesicles with an average diameter of 50 nm are phosphorylated 100 times faster than chemically identical vesicles with an average diameter greater than 300 nm. The low reactivity of large vesicles is not due to the difference in vesicle number for large and small vesicles at constant total lipid, nor to occlusion of lipid surfaces in multilammelar structures, and can be reversed by addition of low (< 1 : 100) molar ratios of either the PtdIns transfer protein sec14p or a ten‐residue peptide derived from the inositol‐phospholipid‐binding site of gelsolin. Similar measurements using PI 4‐kinase showed a weak dependence on vesicle size. The strong dependence of PI 3‐kinase function on membrane curvature suggests possible localization of PI 3‐kinase activity at sites where clustering of receptors, for example, may locally deform the membrane, and suggests that once PI 3‐kinase is localized and activated at surface sites, the reaction may become self‐accelerating.</abstract><cop>Berlin & Heidelberg</cop><pub>Springer‐Verlag</pub><pmid>9874255</pmid><doi>10.1046/j.1432-1327.1998.2580846.x</doi><tpages>8</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 1998-12, Vol.258 (2), p.846-853 |
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| subjects | 1-Phosphatidylinositol 4-Kinase - metabolism Adenosine Triphosphate - metabolism Animals Carrier Proteins - metabolism curvature Drug Compounding Enzyme Activation Fluorescent Dyes - metabolism gelsolin Gelsolin - chemistry inositolphospholipid Lipid Bilayers - metabolism Liposomes - metabolism Liver - enzymology Membrane Proteins Particle Size Peptide Fragments - metabolism Peptides - pharmacology phosphatidylinositol Phosphatidylinositol 3-Kinases - metabolism Phosphatidylinositols - metabolism Phospholipid Transfer Proteins PI 3‐kinase Rats Surface Properties |
| title | Enhancement of phosphoinositide 3‐kinase (PI 3‐kinase) activity by membrane curvature and inositol‐phospholipid‐binding peptides |
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