Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi
Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P...
Gespeichert in:
| Veröffentlicht in: | Cell 2003-08, Vol.114 (3), p.299-310 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 310 |
|---|---|
| container_issue | 3 |
| container_start_page | 299 |
| container_title | Cell |
| container_volume | 114 |
| creator | Wang, Ying Jie Wang, Jing Sun, Hui Qiao Martinez, Manuel Sun, Yu Xiao Macia, Eric Kirchhausen, Tomas Albanesi, Joseph P. Roth, Michael G. Yin, Helen L. |
| description | Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery. |
| doi_str_mv | 10.1016/S0092-8674(03)00603-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_73552978</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0092867403006032</els_id><sourcerecordid>73552978</sourcerecordid><originalsourceid>FETCH-LOGICAL-c557t-b909b253b5f372666c02b63569d28de8dd3395ab10da265b72c37cb6754737b73</originalsourceid><addsrcrecordid>eNqFkUFvEzEQhS1ERUPhJ4B8QnBYOrbX9vqEoggKUqVWUM7W2p4kRpv1YjsV_ffdNgGOPc3o6Xsz0nuEvGHwkQFT5z8ADG86pdv3ID4AKBANf0YWDIxuWqb5c7L4h5ySl6X8AoBOSvmCnDJuWKuMXJBwvU1l2vY1hrshjqnEmgba0r8y0u-42Q_zUuhNnzdY47ihaU1Xs7bNcaTL0E81Zbq8bhhdpd004J8ZronWLdKLNGziK3Ky7oeCr4_zjPz88vlm9bW5vLr4tlpeNl5KXRtnwDguhZNroblSygN3SkhlAu8CdiEIYWTvGISeK-k090J7p7RstdBOizPy7nB3yun3Hku1u1g8DkM_YtoXq4WU3OjuSZB1HdNSmBmUB9DnVErGtZ1y3PX5zjKwDz3Yxx7sQ8gWhH3swfLZ9_b4YO92GP67jsHPwKcDgHMetxGzLT7i6DHEjL7akOITL-4BjAGWyA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18817539</pqid></control><display><type>article</type><title>Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Wang, Ying Jie ; Wang, Jing ; Sun, Hui Qiao ; Martinez, Manuel ; Sun, Yu Xiao ; Macia, Eric ; Kirchhausen, Tomas ; Albanesi, Joseph P. ; Roth, Michael G. ; Yin, Helen L.</creator><creatorcontrib>Wang, Ying Jie ; Wang, Jing ; Sun, Hui Qiao ; Martinez, Manuel ; Sun, Yu Xiao ; Macia, Eric ; Kirchhausen, Tomas ; Albanesi, Joseph P. ; Roth, Michael G. ; Yin, Helen L.</creatorcontrib><description>Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(03)00603-2</identifier><identifier>PMID: 12914695</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adaptor Protein Complex 1 - metabolism ; Animals ; Biomarkers ; Cell Membrane - metabolism ; Clathrin - metabolism ; COS Cells ; Exocytosis - physiology ; Golgi Apparatus - metabolism ; HeLa Cells ; Humans ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Phosphatidylinositol 4,5-Diphosphate - metabolism ; Phosphatidylinositol Phosphates - metabolism ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Protein Binding ; Protein Transport - physiology ; Recombinant Fusion Proteins - metabolism ; RNA Interference</subject><ispartof>Cell, 2003-08, Vol.114 (3), p.299-310</ispartof><rights>2003 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-b909b253b5f372666c02b63569d28de8dd3395ab10da265b72c37cb6754737b73</citedby><cites>FETCH-LOGICAL-c557t-b909b253b5f372666c02b63569d28de8dd3395ab10da265b72c37cb6754737b73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867403006032$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12914695$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Ying Jie</creatorcontrib><creatorcontrib>Wang, Jing</creatorcontrib><creatorcontrib>Sun, Hui Qiao</creatorcontrib><creatorcontrib>Martinez, Manuel</creatorcontrib><creatorcontrib>Sun, Yu Xiao</creatorcontrib><creatorcontrib>Macia, Eric</creatorcontrib><creatorcontrib>Kirchhausen, Tomas</creatorcontrib><creatorcontrib>Albanesi, Joseph P.</creatorcontrib><creatorcontrib>Roth, Michael G.</creatorcontrib><creatorcontrib>Yin, Helen L.</creatorcontrib><title>Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi</title><title>Cell</title><addtitle>Cell</addtitle><description>Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.</description><subject>Adaptor Protein Complex 1 - metabolism</subject><subject>Animals</subject><subject>Biomarkers</subject><subject>Cell Membrane - metabolism</subject><subject>Clathrin - metabolism</subject><subject>COS Cells</subject><subject>Exocytosis - physiology</subject><subject>Golgi Apparatus - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Phosphatidylinositol 4,5-Diphosphate - metabolism</subject><subject>Phosphatidylinositol Phosphates - metabolism</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Protein Binding</subject><subject>Protein Transport - physiology</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA Interference</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFvEzEQhS1ERUPhJ4B8QnBYOrbX9vqEoggKUqVWUM7W2p4kRpv1YjsV_ffdNgGOPc3o6Xsz0nuEvGHwkQFT5z8ADG86pdv3ID4AKBANf0YWDIxuWqb5c7L4h5ySl6X8AoBOSvmCnDJuWKuMXJBwvU1l2vY1hrshjqnEmgba0r8y0u-42Q_zUuhNnzdY47ihaU1Xs7bNcaTL0E81Zbq8bhhdpd004J8ZronWLdKLNGziK3Ky7oeCr4_zjPz88vlm9bW5vLr4tlpeNl5KXRtnwDguhZNroblSygN3SkhlAu8CdiEIYWTvGISeK-k090J7p7RstdBOizPy7nB3yun3Hku1u1g8DkM_YtoXq4WU3OjuSZB1HdNSmBmUB9DnVErGtZ1y3PX5zjKwDz3Yxx7sQ8gWhH3swfLZ9_b4YO92GP67jsHPwKcDgHMetxGzLT7i6DHEjL7akOITL-4BjAGWyA</recordid><startdate>20030808</startdate><enddate>20030808</enddate><creator>Wang, Ying Jie</creator><creator>Wang, Jing</creator><creator>Sun, Hui Qiao</creator><creator>Martinez, Manuel</creator><creator>Sun, Yu Xiao</creator><creator>Macia, Eric</creator><creator>Kirchhausen, Tomas</creator><creator>Albanesi, Joseph P.</creator><creator>Roth, Michael G.</creator><creator>Yin, Helen L.</creator><general>Elsevier Inc</general><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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20030808</creationdate><title>Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi</title><author>Wang, Ying Jie ; Wang, Jing ; Sun, Hui Qiao ; Martinez, Manuel ; Sun, Yu Xiao ; Macia, Eric ; Kirchhausen, Tomas ; Albanesi, Joseph P. ; Roth, Michael G. ; Yin, Helen L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-b909b253b5f372666c02b63569d28de8dd3395ab10da265b72c37cb6754737b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adaptor Protein Complex 1 - metabolism</topic><topic>Animals</topic><topic>Biomarkers</topic><topic>Cell Membrane - metabolism</topic><topic>Clathrin - metabolism</topic><topic>COS Cells</topic><topic>Exocytosis - physiology</topic><topic>Golgi Apparatus - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Phosphatidylinositol 4,5-Diphosphate - metabolism</topic><topic>Phosphatidylinositol Phosphates - metabolism</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>Protein Binding</topic><topic>Protein Transport - physiology</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RNA Interference</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Ying Jie</creatorcontrib><creatorcontrib>Wang, Jing</creatorcontrib><creatorcontrib>Sun, Hui Qiao</creatorcontrib><creatorcontrib>Martinez, Manuel</creatorcontrib><creatorcontrib>Sun, Yu Xiao</creatorcontrib><creatorcontrib>Macia, Eric</creatorcontrib><creatorcontrib>Kirchhausen, Tomas</creatorcontrib><creatorcontrib>Albanesi, Joseph P.</creatorcontrib><creatorcontrib>Roth, Michael G.</creatorcontrib><creatorcontrib>Yin, Helen L.</creatorcontrib><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>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Ying Jie</au><au>Wang, Jing</au><au>Sun, Hui Qiao</au><au>Martinez, Manuel</au><au>Sun, Yu Xiao</au><au>Macia, Eric</au><au>Kirchhausen, Tomas</au><au>Albanesi, Joseph P.</au><au>Roth, Michael G.</au><au>Yin, Helen L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2003-08-08</date><risdate>2003</risdate><volume>114</volume><issue>3</issue><spage>299</spage><epage>310</epage><pages>299-310</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12914695</pmid><doi>10.1016/S0092-8674(03)00603-2</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 2003-08, Vol.114 (3), p.299-310 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73552978 |
| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Adaptor Protein Complex 1 - metabolism Animals Biomarkers Cell Membrane - metabolism Clathrin - metabolism COS Cells Exocytosis - physiology Golgi Apparatus - metabolism HeLa Cells Humans Isoenzymes - genetics Isoenzymes - metabolism Phosphatidylinositol 4,5-Diphosphate - metabolism Phosphatidylinositol Phosphates - metabolism Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein Binding Protein Transport - physiology Recombinant Fusion Proteins - metabolism RNA Interference |
| title | Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T06%3A51%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phosphatidylinositol%204%20Phosphate%20Regulates%20Targeting%20of%20Clathrin%20Adaptor%20AP-1%20Complexes%20to%20the%20Golgi&rft.jtitle=Cell&rft.au=Wang,%20Ying%20Jie&rft.date=2003-08-08&rft.volume=114&rft.issue=3&rft.spage=299&rft.epage=310&rft.pages=299-310&rft.issn=0092-8674&rft.eissn=1097-4172&rft_id=info:doi/10.1016/S0092-8674(03)00603-2&rft_dat=%3Cproquest_cross%3E73552978%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=18817539&rft_id=info:pmid/12914695&rft_els_id=S0092867403006032&rfr_iscdi=true |