EEA1 links PI(3)K function to rab5 regulation of endosome fusion.

Research output: Contribution to journalArticlepeer-review

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EEA1 links PI(3)K function to rab5 regulation of endosome fusion. / Simonsen, A.; Lippe, R.; Christoforidis, S.; Gaullier, J-M.; Brech, A.; Callaghan, J.; Toh, B-H.; Murphy, C.; Zerial, M.; Stenmark, H.

In: Nature, Vol. 394, 1998, p. 494-498.

Research output: Contribution to journalArticlepeer-review

Harvard

Simonsen, A, Lippe, R, Christoforidis, S, Gaullier, J-M, Brech, A, Callaghan, J, Toh, B-H, Murphy, C, Zerial, M & Stenmark, H 1998, 'EEA1 links PI(3)K function to rab5 regulation of endosome fusion.', Nature, vol. 394, pp. 494-498.

APA

Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J-M., Brech, A., Callaghan, J., Toh, B-H., Murphy, C., Zerial, M., & Stenmark, H. (1998). EEA1 links PI(3)K function to rab5 regulation of endosome fusion. Nature, 394, 494-498.

Vancouver

Simonsen A, Lippe R, Christoforidis S, Gaullier J-M, Brech A, Callaghan J et al. EEA1 links PI(3)K function to rab5 regulation of endosome fusion. Nature. 1998;394:494-498.

Author

Simonsen, A. ; Lippe, R. ; Christoforidis, S. ; Gaullier, J-M. ; Brech, A. ; Callaghan, J. ; Toh, B-H. ; Murphy, C. ; Zerial, M. ; Stenmark, H. / EEA1 links PI(3)K function to rab5 regulation of endosome fusion. In: Nature. 1998 ; Vol. 394. pp. 494-498.

Bibtex

@article{a24c8fa2a20d46f8b86fceaa26134a72,
title = "EEA1 links PI(3)K function to rab5 regulation of endosome fusion.",
abstract = "GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood. Fusion between early endosomes requires phosphatidylinositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5. Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited. Here we identify the early-endosomal autoantigen EEA1 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.",
keywords = "1-Phosphatidylinositol 3-Kinase/antagonists & inhibitors/*physiology Androstadienes/pharmacology Animal Autoantigens/physiology Cattle Cell Line Cloning, Molecular Endosomes/*physiology Enzyme Inhibitors/pharmacology GTP-Binding Proteins/genetics/*physiology Guanosine Triphosphate/physiology Hamsters Hela Cells Human Intracellular Membranes/physiology Membrane Fusion/*physiology Membrane Proteins/genetics/*physiology Mutagenesis Recombinant Fusion Proteins/metabolism Support, Non-U.S. Gov't rab5 GTP-Binding Proteins/*metabolism",
author = "A. Simonsen and R. Lippe and S. Christoforidis and J-M. Gaullier and A. Brech and J. Callaghan and B-H. Toh and C. Murphy and M. Zerial and H. Stenmark",
year = "1998",
language = "English",
volume = "394",
pages = "494--498",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - EEA1 links PI(3)K function to rab5 regulation of endosome fusion.

AU - Simonsen, A.

AU - Lippe, R.

AU - Christoforidis, S.

AU - Gaullier, J-M.

AU - Brech, A.

AU - Callaghan, J.

AU - Toh, B-H.

AU - Murphy, C.

AU - Zerial, M.

AU - Stenmark, H.

PY - 1998

Y1 - 1998

N2 - GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood. Fusion between early endosomes requires phosphatidylinositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5. Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited. Here we identify the early-endosomal autoantigen EEA1 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.

AB - GTPases and lipid kinases regulate membrane traffic along the endocytic pathway by mechanisms that are not completely understood. Fusion between early endosomes requires phosphatidylinositol-3-OH kinase (PI(3)K) activity as well as the small GTPase Rab5. Excess Rab5-GTP complex restores endosome fusion when PI(3)K is inhibited. Here we identify the early-endosomal autoantigen EEA1 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.

KW - 1-Phosphatidylinositol 3-Kinase/antagonists & inhibitors/physiology Androstadienes/pharmacology Animal Autoantigens/physiology Cattle Cell Line Cloning, Molecular Endosomes/physiology Enzyme Inhibitors/pharmacology GTP-Binding Proteins/genetics/physiology

M3 - Article

VL - 394

SP - 494

EP - 498

JO - Nature

JF - Nature

SN - 0028-0836

ER -