Analysis of Phosphoinositide-Binding Properties and Subcellular Localization of GFP-Fusion Proteins
Specific protein-phosphoinositide (PI) interactions are known to play a key role in the targeting of proteins to specific cellular membranes. Investigation of these interactions would be greatly facilitated if GFP-fusion proteins expressed in mammalian cells and used for their subcellular localizati...
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| Veröffentlicht in: | Lipids 2015-04, Vol.50 (4), p.427-436 |
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| creator | Jun, Yong-Woo Kim, Sangyeol Kim, Kun-Hyung Lee, Jin-A Lim, Chae-Seok Chang, Iksoo Suh, Byung-Chang Kaang, Bong-Kiun Jang, Deok-Jin |
| description | Specific protein-phosphoinositide (PI) interactions are known to play a key role in the targeting of proteins to specific cellular membranes. Investigation of these interactions would be greatly facilitated if GFP-fusion proteins expressed in mammalian cells and used for their subcellular localization could also be employed for in vitro lipid binding. In this study, we found that lysates of cells overexpressing GFP-fusion proteins could be used for in vitro protein-PI binding assays. We applied this approach to examine the PI-binding properties of
Aplysia
Sec7 protein (ApSec7) and its isoform ApSec7(VPKIS), in which a VPKIS sequence is inserted into the PH domain of ApSec7. EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did specifically bind to PI(3,4,5)P
3
in an in vitro lipid-coated bead assay. Overexpression of EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did induce neurite outgrowth in
Aplysia
sensory neurons. Structure modeling analysis revealed that the inserted VPKIS caused misfolding around the PI(3,4,5)P
3
-binding pocket of ApSec7 and disturbed the binding of PI(3,4,5)P
3
to the pleckstrin homology (PH) domain. Our data indicate that plasma membrane localization of EGFP-ApSec7 via the interaction between its PH domain and PI(3,4,5)P
3
might play a key role in neurite outgrowth in
Aplysia
. |
| doi_str_mv | 10.1007/s11745-015-3994-z |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1665121553</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1665121553</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4907-c579c935e32459662db0760d35fcde9f726abea9bce5fab6e3fa4ad2637c26ab3</originalsourceid><addsrcrecordid>eNqFkV9rFDEUxYModq1-AF9kwBdfovmfzWOtbi0suKA-h0wm06bMJmvuDGX305txqoggPoVLfufcwz0IvaTkLSVEvwNKtZCYUIm5MQKfHqEVlXKNDSf6MVoRwgQWjNAz9Azgro5UGPkUnTGp1mvC1Ar5i-SGI0Roct_sbjMcbnNMGeIYu4Dfx9TFdNPsSj6EMsYAjUtd82VqfRiGaXCl2WbvhnhyY8xp9rja7PBmgnmqqjHEBM_Rk94NEF48vOfo2-bj18tPePv56vryYou9MERjL7XxhsvAmZBGKda1RCvScdn7LpheM-Xa4EzdLXvXqsB7J1zHFNd-_uLn6M3ieyj5-xRgtPsIc1CXQp7AUqUkZfVAvKKv_0Lv8lTqKX5SQnBq9EzRhfIlA5TQ20OJe1eOlhI7N2CXBmxtwM4N2FPVvHpwntp96H4rfp28AnoB7uMQjv93tNvr3QcimK5KtiihitJNKH-E_meeH7L5ozM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1664431973</pqid></control><display><type>article</type><title>Analysis of Phosphoinositide-Binding Properties and Subcellular Localization of GFP-Fusion Proteins</title><source>MEDLINE</source><source>Wiley Online Library All Journals</source><source>SpringerLink Journals - AutoHoldings</source><creator>Jun, Yong-Woo ; Kim, Sangyeol ; Kim, Kun-Hyung ; Lee, Jin-A ; Lim, Chae-Seok ; Chang, Iksoo ; Suh, Byung-Chang ; Kaang, Bong-Kiun ; Jang, Deok-Jin</creator><creatorcontrib>Jun, Yong-Woo ; Kim, Sangyeol ; Kim, Kun-Hyung ; Lee, Jin-A ; Lim, Chae-Seok ; Chang, Iksoo ; Suh, Byung-Chang ; Kaang, Bong-Kiun ; Jang, Deok-Jin</creatorcontrib><description>Specific protein-phosphoinositide (PI) interactions are known to play a key role in the targeting of proteins to specific cellular membranes. Investigation of these interactions would be greatly facilitated if GFP-fusion proteins expressed in mammalian cells and used for their subcellular localization could also be employed for in vitro lipid binding. In this study, we found that lysates of cells overexpressing GFP-fusion proteins could be used for in vitro protein-PI binding assays. We applied this approach to examine the PI-binding properties of
Aplysia
Sec7 protein (ApSec7) and its isoform ApSec7(VPKIS), in which a VPKIS sequence is inserted into the PH domain of ApSec7. EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did specifically bind to PI(3,4,5)P
3
in an in vitro lipid-coated bead assay. Overexpression of EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did induce neurite outgrowth in
Aplysia
sensory neurons. Structure modeling analysis revealed that the inserted VPKIS caused misfolding around the PI(3,4,5)P
3
-binding pocket of ApSec7 and disturbed the binding of PI(3,4,5)P
3
to the pleckstrin homology (PH) domain. Our data indicate that plasma membrane localization of EGFP-ApSec7 via the interaction between its PH domain and PI(3,4,5)P
3
might play a key role in neurite outgrowth in
Aplysia
.</description><identifier>ISSN: 0024-4201</identifier><identifier>EISSN: 1558-9307</identifier><identifier>DOI: 10.1007/s11745-015-3994-z</identifier><identifier>PMID: 25688026</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amino Acid Sequence ; Animals ; Aplysia - cytology ; Aplysia - genetics ; Aplysia - metabolism ; Aplysia Sec7 ; Biomedical and Life Sciences ; GFP‐fusion protein ; Green Fluorescent Proteins - analysis ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; HEK293 Cells ; Humans ; In vitro protein‐phosphoinositide binding ; Life Sciences ; Lipidology ; Medical Biochemistry ; Medicinal Chemistry ; Methods ; Microbial Genetics and Genomics ; Models, Molecular ; Molecular Sequence Data ; Neurite outgrowth ; Neurochemistry ; Nutrition ; Phosphatidylinositols - metabolism ; Phosphoinositide ; PI(3,4,5)P3 ; Protein Binding ; Proteins ; Recombinant Fusion Proteins - analysis ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism</subject><ispartof>Lipids, 2015-04, Vol.50 (4), p.427-436</ispartof><rights>AOCS 2015</rights><rights>2015 American Oil Chemists' Society (AOCS)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4907-c579c935e32459662db0760d35fcde9f726abea9bce5fab6e3fa4ad2637c26ab3</citedby><cites>FETCH-LOGICAL-c4907-c579c935e32459662db0760d35fcde9f726abea9bce5fab6e3fa4ad2637c26ab3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11745-015-3994-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11745-015-3994-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,41488,42557,45574,45575,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25688026$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jun, Yong-Woo</creatorcontrib><creatorcontrib>Kim, Sangyeol</creatorcontrib><creatorcontrib>Kim, Kun-Hyung</creatorcontrib><creatorcontrib>Lee, Jin-A</creatorcontrib><creatorcontrib>Lim, Chae-Seok</creatorcontrib><creatorcontrib>Chang, Iksoo</creatorcontrib><creatorcontrib>Suh, Byung-Chang</creatorcontrib><creatorcontrib>Kaang, Bong-Kiun</creatorcontrib><creatorcontrib>Jang, Deok-Jin</creatorcontrib><title>Analysis of Phosphoinositide-Binding Properties and Subcellular Localization of GFP-Fusion Proteins</title><title>Lipids</title><addtitle>Lipids</addtitle><addtitle>Lipids</addtitle><description>Specific protein-phosphoinositide (PI) interactions are known to play a key role in the targeting of proteins to specific cellular membranes. Investigation of these interactions would be greatly facilitated if GFP-fusion proteins expressed in mammalian cells and used for their subcellular localization could also be employed for in vitro lipid binding. In this study, we found that lysates of cells overexpressing GFP-fusion proteins could be used for in vitro protein-PI binding assays. We applied this approach to examine the PI-binding properties of
Aplysia
Sec7 protein (ApSec7) and its isoform ApSec7(VPKIS), in which a VPKIS sequence is inserted into the PH domain of ApSec7. EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did specifically bind to PI(3,4,5)P
3
in an in vitro lipid-coated bead assay. Overexpression of EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did induce neurite outgrowth in
Aplysia
sensory neurons. Structure modeling analysis revealed that the inserted VPKIS caused misfolding around the PI(3,4,5)P
3
-binding pocket of ApSec7 and disturbed the binding of PI(3,4,5)P
3
to the pleckstrin homology (PH) domain. Our data indicate that plasma membrane localization of EGFP-ApSec7 via the interaction between its PH domain and PI(3,4,5)P
3
might play a key role in neurite outgrowth in
Aplysia
.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aplysia - cytology</subject><subject>Aplysia - genetics</subject><subject>Aplysia - metabolism</subject><subject>Aplysia Sec7</subject><subject>Biomedical and Life Sciences</subject><subject>GFP‐fusion protein</subject><subject>Green Fluorescent Proteins - analysis</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>In vitro protein‐phosphoinositide binding</subject><subject>Life Sciences</subject><subject>Lipidology</subject><subject>Medical Biochemistry</subject><subject>Medicinal Chemistry</subject><subject>Methods</subject><subject>Microbial Genetics and Genomics</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Neurite outgrowth</subject><subject>Neurochemistry</subject><subject>Nutrition</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Phosphoinositide</subject><subject>PI(3,4,5)P3</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - analysis</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><issn>0024-4201</issn><issn>1558-9307</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</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>eNqFkV9rFDEUxYModq1-AF9kwBdfovmfzWOtbi0suKA-h0wm06bMJmvuDGX305txqoggPoVLfufcwz0IvaTkLSVEvwNKtZCYUIm5MQKfHqEVlXKNDSf6MVoRwgQWjNAz9Azgro5UGPkUnTGp1mvC1Ar5i-SGI0Roct_sbjMcbnNMGeIYu4Dfx9TFdNPsSj6EMsYAjUtd82VqfRiGaXCl2WbvhnhyY8xp9rja7PBmgnmqqjHEBM_Rk94NEF48vOfo2-bj18tPePv56vryYou9MERjL7XxhsvAmZBGKda1RCvScdn7LpheM-Xa4EzdLXvXqsB7J1zHFNd-_uLn6M3ieyj5-xRgtPsIc1CXQp7AUqUkZfVAvKKv_0Lv8lTqKX5SQnBq9EzRhfIlA5TQ20OJe1eOlhI7N2CXBmxtwM4N2FPVvHpwntp96H4rfp28AnoB7uMQjv93tNvr3QcimK5KtiihitJNKH-E_meeH7L5ozM</recordid><startdate>201504</startdate><enddate>201504</enddate><creator>Jun, Yong-Woo</creator><creator>Kim, Sangyeol</creator><creator>Kim, Kun-Hyung</creator><creator>Lee, Jin-A</creator><creator>Lim, Chae-Seok</creator><creator>Chang, Iksoo</creator><creator>Suh, Byung-Chang</creator><creator>Kaang, Bong-Kiun</creator><creator>Jang, Deok-Jin</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</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>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</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>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>201504</creationdate><title>Analysis of Phosphoinositide-Binding Properties and Subcellular Localization of GFP-Fusion Proteins</title><author>Jun, Yong-Woo ; Kim, Sangyeol ; Kim, Kun-Hyung ; Lee, Jin-A ; Lim, Chae-Seok ; Chang, Iksoo ; Suh, Byung-Chang ; Kaang, Bong-Kiun ; Jang, Deok-Jin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4907-c579c935e32459662db0760d35fcde9f726abea9bce5fab6e3fa4ad2637c26ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aplysia - cytology</topic><topic>Aplysia - genetics</topic><topic>Aplysia - metabolism</topic><topic>Aplysia Sec7</topic><topic>Biomedical and Life Sciences</topic><topic>GFP‐fusion protein</topic><topic>Green Fluorescent Proteins - analysis</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>In vitro protein‐phosphoinositide binding</topic><topic>Life Sciences</topic><topic>Lipidology</topic><topic>Medical Biochemistry</topic><topic>Medicinal Chemistry</topic><topic>Methods</topic><topic>Microbial Genetics and Genomics</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Neurite outgrowth</topic><topic>Neurochemistry</topic><topic>Nutrition</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Phosphoinositide</topic><topic>PI(3,4,5)P3</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - analysis</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jun, Yong-Woo</creatorcontrib><creatorcontrib>Kim, Sangyeol</creatorcontrib><creatorcontrib>Kim, Kun-Hyung</creatorcontrib><creatorcontrib>Lee, Jin-A</creatorcontrib><creatorcontrib>Lim, Chae-Seok</creatorcontrib><creatorcontrib>Chang, Iksoo</creatorcontrib><creatorcontrib>Suh, Byung-Chang</creatorcontrib><creatorcontrib>Kaang, Bong-Kiun</creatorcontrib><creatorcontrib>Jang, Deok-Jin</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 Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</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 Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic 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>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Lipids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jun, Yong-Woo</au><au>Kim, Sangyeol</au><au>Kim, Kun-Hyung</au><au>Lee, Jin-A</au><au>Lim, Chae-Seok</au><au>Chang, Iksoo</au><au>Suh, Byung-Chang</au><au>Kaang, Bong-Kiun</au><au>Jang, Deok-Jin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of Phosphoinositide-Binding Properties and Subcellular Localization of GFP-Fusion Proteins</atitle><jtitle>Lipids</jtitle><stitle>Lipids</stitle><addtitle>Lipids</addtitle><date>2015-04</date><risdate>2015</risdate><volume>50</volume><issue>4</issue><spage>427</spage><epage>436</epage><pages>427-436</pages><issn>0024-4201</issn><eissn>1558-9307</eissn><abstract>Specific protein-phosphoinositide (PI) interactions are known to play a key role in the targeting of proteins to specific cellular membranes. Investigation of these interactions would be greatly facilitated if GFP-fusion proteins expressed in mammalian cells and used for their subcellular localization could also be employed for in vitro lipid binding. In this study, we found that lysates of cells overexpressing GFP-fusion proteins could be used for in vitro protein-PI binding assays. We applied this approach to examine the PI-binding properties of
Aplysia
Sec7 protein (ApSec7) and its isoform ApSec7(VPKIS), in which a VPKIS sequence is inserted into the PH domain of ApSec7. EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did specifically bind to PI(3,4,5)P
3
in an in vitro lipid-coated bead assay. Overexpression of EGFP-ApSec7 but not EGFP-ApSec7(VPKIS) did induce neurite outgrowth in
Aplysia
sensory neurons. Structure modeling analysis revealed that the inserted VPKIS caused misfolding around the PI(3,4,5)P
3
-binding pocket of ApSec7 and disturbed the binding of PI(3,4,5)P
3
to the pleckstrin homology (PH) domain. Our data indicate that plasma membrane localization of EGFP-ApSec7 via the interaction between its PH domain and PI(3,4,5)P
3
might play a key role in neurite outgrowth in
Aplysia
.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>25688026</pmid><doi>10.1007/s11745-015-3994-z</doi><tpages>10</tpages></addata></record> |
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| ispartof | Lipids, 2015-04, Vol.50 (4), p.427-436 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_1665121553 |
| source | MEDLINE; Wiley Online Library All Journals; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Animals Aplysia - cytology Aplysia - genetics Aplysia - metabolism Aplysia Sec7 Biomedical and Life Sciences GFP‐fusion protein Green Fluorescent Proteins - analysis Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism HEK293 Cells Humans In vitro protein‐phosphoinositide binding Life Sciences Lipidology Medical Biochemistry Medicinal Chemistry Methods Microbial Genetics and Genomics Models, Molecular Molecular Sequence Data Neurite outgrowth Neurochemistry Nutrition Phosphatidylinositols - metabolism Phosphoinositide PI(3,4,5)P3 Protein Binding Proteins Recombinant Fusion Proteins - analysis Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism |
| title | Analysis of Phosphoinositide-Binding Properties and Subcellular Localization of GFP-Fusion Proteins |
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