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

Author

Listed:
  • Anne Simonsen

    (The Norwegian Radium Hospital)

  • Roger Lippe

    (EMBL
    Max Planck Institute for Molecular Cell Biology and Genetics)

  • Savvas Christoforidis

    (EMBL
    Max Planck Institute for Molecular Cell Biology and Genetics)

  • 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
    Max Planck Institute for Molecular Cell Biology and Genetics
    University of Ioannina Medical School)

  • Marino Zerial

    (EMBL
    Max Planck Institute for Molecular Cell Biology and Genetics)

  • Harald Stenmark

    (The Norwegian Radium Hospital)

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.

Suggested Citation

  • Anne Simonsen & Roger Lippe & Savvas Christoforidis & Jean-Michel Gaullier & Andreas Brech & Judy Callaghan & Ban-Hock Toh & Carol Murphy & Marino Zerial & Harald Stenmark, 1998. "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion," Nature, Nature, vol. 394(6692), pages 494-498, July.
    • Handle: RePEc:nat:nature:v:394:y:1998:i:6692:d:10.1038_28879
    DOI: 10.1038/28879
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    Cited by:

    1. Oliver M Crook & Aikaterini Geladaki & Daniel J H Nightingale & Owen L Vennard & Kathryn S Lilley & Laurent Gatto & Paul D W Kirk, 2020. "A semi-supervised Bayesian approach for simultaneous protein sub-cellular localisation assignment and novelty detection," PLOS Computational Biology, Public Library of Science, vol. 16(11), pages 1-21, November.
    2. Hui Tu & Zhimeng Wang & Ye Yuan & Xilin Miao & Dong Li & Hu Guo & Yihong Yang & Huaqing Cai, 2022. "The PripA-TbcrA complex-centered Rab GAP cascade facilitates macropinosome maturation in Dictyostelium," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Eva Maria Wenzel & Nina Marie Pedersen & Liv Anker Elfmark & Ling Wang & Ingrid Kjos & Espen Stang & Lene Malerød & Andreas Brech & Harald Stenmark & Camilla Raiborg, 2024. "Intercellular transfer of cancer cell invasiveness via endosome-mediated protease shedding," Nature Communications, Nature, vol. 15(1), pages 1-22, December.

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