EEA1 links PI(3)K function to Rab5 regulation of endosome fusion

Anne Simonsen, Roger Lippe, Savvas Christoforidis, Jean-Michel Gaullier, Andreas Brech, Judy Callaghan, Ban-Hock Toh, Carol Murphy, Marino Zerial and Harald Stenmark ()
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Anne Simonsen: The Norwegian Radium Hospital
Roger Lippe: EMBL
Savvas Christoforidis: EMBL
Jean-Michel Gaullier: The Norwegian Radium Hospital
Andreas Brech: EM-unit, Institute of Biology
Judy Callaghan: Monash Medical School
Ban-Hock Toh: Monash Medical School
Carol Murphy: EMBL
Marino Zerial: EMBL
Harald Stenmark: The Norwegian Radium Hospital

Nature, 1998, vol. 394, issue 6692, 494-498

Abstract: Abstract GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood1,2,3,4. Fusion between early endosomes requires phosphatidyl-inositol-3-OH kinase (PI(3)K) activity5,6,7 as well as the small GTPase Rab5 (ref. 8). Excess Rab5–GTP complex restores endosome fusion when PI(3)K is inhibited5,9. Here we identify the early-endosomal autoantigen EEA1 (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 endosomes10 indicates that EEA1 may confer directionality to Rab5-dependent endocytic transport.

Date: 1998
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DOI: 10.1038/28879

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