EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood. Fusion between early endosomes requires phosphatidyl-inositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5 (ref. 8). Excess Rab5-GTP complex restores en...
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| Veröffentlicht in: | Nature (London) 1998-07, Vol.394 (6692), p.494-498 |
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| creator | Stenmark, Harald Simonsen, Anne Lippe, Roger Christoforidis, Savvas Gaullier, Jean-Michel Brech, Andreas Callaghan, Judy Toh, Ban-Hock Murphy, Carol Zerial, Marino |
| description | GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood. Fusion between early endosomes requires phosphatidyl-inositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5 (ref. 8). Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited,. Here we identify the early-endosomal autoantigen EEA1 (refs 10-12) which binds the PI(3)K product phosphatidylinositol-3-phosphate, as a new Rab5 effector that is required for endosome fusion. The association of EEA1 with the endosomal membrane requires Rab5-GTP and PI(3)K activity, and excess Rab5-GTP stabilizes the membrane association of EEA1 even when PI(3)K is inhibited. The identification of EEA1 as a direct Rab5 effector provides a molecular link between PI(3)K and Rab5, and its restricted distribution to early endosomes indicates that EEA1 may confer directionality to Rab5-dependent endocytic transport. |
| doi_str_mv | 10.1038/28879 |
| format | Article |
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Fusion between early endosomes requires phosphatidyl-inositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5 (ref. 8). Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited,. Here we identify the early-endosomal autoantigen EEA1 (refs 10-12) which binds the PI(3)K product phosphatidylinositol-3-phosphate, as a new Rab5 effector that is required for endosome fusion. The association of EEA1 with the endosomal membrane requires Rab5-GTP and PI(3)K activity, and excess Rab5-GTP stabilizes the membrane association of EEA1 even when PI(3)K is inhibited. The identification of EEA1 as a direct Rab5 effector provides a molecular link between PI(3)K and Rab5, and its restricted distribution to early endosomes indicates that EEA1 may confer directionality to Rab5-dependent endocytic transport.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/28879</identifier><identifier>PMID: 9697774</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Androstadienes - pharmacology ; Animals ; Autoantigens - physiology ; Biochemistry ; Biological and medical sciences ; Cattle ; Cell Line ; Cell physiology ; Cloning, Molecular ; Cricetinae ; Endocytosis ; Endosomes - physiology ; Enzyme Inhibitors - pharmacology ; Fundamental and applied biological sciences. Psychology ; GTP-Binding Proteins - genetics ; GTP-Binding Proteins - physiology ; Guanosine Triphosphate - physiology ; HeLa Cells ; Humanities and Social Sciences ; Humans ; Intracellular Membranes - physiology ; letter ; Membrane Fusion - physiology ; Membrane Proteins - genetics ; Membrane Proteins - physiology ; Membranes ; Molecular and cellular biology ; multidisciplinary ; Mutagenesis ; Phosphatidylinositol 3-Kinases - antagonists & inhibitors ; Phosphatidylinositol 3-Kinases - physiology ; rab5 GTP-Binding Proteins ; Recombinant Fusion Proteins - metabolism ; Science ; Science (multidisciplinary) ; Vesicular Transport Proteins</subject><ispartof>Nature (London), 1998-07, Vol.394 (6692), p.494-498</ispartof><rights>Macmillan Magazines Ltd. 1998</rights><rights>1998 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. 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Fusion between early endosomes requires phosphatidyl-inositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5 (ref. 8). Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited,. Here we identify the early-endosomal autoantigen EEA1 (refs 10-12) which binds the PI(3)K product phosphatidylinositol-3-phosphate, as a new Rab5 effector that is required for endosome fusion. The association of EEA1 with the endosomal membrane requires Rab5-GTP and PI(3)K activity, and excess Rab5-GTP stabilizes the membrane association of EEA1 even when PI(3)K is inhibited. 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Roger</au><au>Christoforidis, Savvas</au><au>Gaullier, Jean-Michel</au><au>Brech, Andreas</au><au>Callaghan, Judy</au><au>Toh, Ban-Hock</au><au>Murphy, Carol</au><au>Zerial, Marino</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>EEA1 links PI(3)K function to Rab5 regulation of endosome fusion</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1998-07-30</date><risdate>1998</risdate><volume>394</volume><issue>6692</issue><spage>494</spage><epage>498</epage><pages>494-498</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood. Fusion between early endosomes requires phosphatidyl-inositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5 (ref. 8). Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited,. Here we identify the early-endosomal autoantigen EEA1 (refs 10-12) which binds the PI(3)K product phosphatidylinositol-3-phosphate, as a new Rab5 effector that is required for endosome fusion. The association of EEA1 with the endosomal membrane requires Rab5-GTP and PI(3)K activity, and excess Rab5-GTP stabilizes the membrane association of EEA1 even when PI(3)K is inhibited. The identification of EEA1 as a direct Rab5 effector provides a molecular link between PI(3)K and Rab5, and its restricted distribution to early endosomes indicates that EEA1 may confer directionality to Rab5-dependent endocytic transport.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>9697774</pmid><doi>10.1038/28879</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1998-07, Vol.394 (6692), p.494-498 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Nature; SpringerLink Journals - AutoHoldings |
| subjects | Androstadienes - pharmacology Animals Autoantigens - physiology Biochemistry Biological and medical sciences Cattle Cell Line Cell physiology Cloning, Molecular Cricetinae Endocytosis Endosomes - physiology Enzyme Inhibitors - pharmacology Fundamental and applied biological sciences. Psychology GTP-Binding Proteins - genetics GTP-Binding Proteins - physiology Guanosine Triphosphate - physiology HeLa Cells Humanities and Social Sciences Humans Intracellular Membranes - physiology letter Membrane Fusion - physiology Membrane Proteins - genetics Membrane Proteins - physiology Membranes Molecular and cellular biology multidisciplinary Mutagenesis Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - physiology rab5 GTP-Binding Proteins Recombinant Fusion Proteins - metabolism Science Science (multidisciplinary) Vesicular Transport Proteins |
| title | EEA1 links PI(3)K function to Rab5 regulation of endosome fusion |
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