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J Biol Chem, Vol. 275, Issue 5, 3699-3705, February 4, 2000
From the Program in Molecular Medicine and the Departments of
Early endosome antigen 1 (EEA1) is 170-kDa
polypeptide required for endosome fusion. EEA1 binds to both
phosphtidylinositol 3-phosphate (PtdIns3P) and to Rab5-GTP in
vitro, but the functional role of this dual interaction at the
endosomal membrane is unclear. Here we have determined the structural
features in EEA1 required for binding to these ligands. We have found
that the FYVE domain is critical for both PtdIns3P and Rab5 binding.
Whereas PtdIns3P binding only required the FYVE domain, Rab5 binding
additionally required a 30-amino acid region directly adjacent to the
FYVE domain. Microinjection of glutathione S-transferase
fusion constructs into Cos cells revealed that the FYVE domain alone is
insufficient for localization to cellular membranes; the upstream
30-amino acid region required for Rab5 binding must also be present for endosomal binding. The importance of Rab5 in membrane binding of EEA1
is underscored by the finding that the increased expression of
wild-type Rab5 increases endosomal binding of EEA1 and decreases its
dependence on PtdIns3P. Thus, the levels of Rab5 are rate-limiting for
the recruitment of EEA1 to endosome membranes. PtdIns3P may play a role
in modulating the Rab5 EEA1 interaction.
The FYVE Domain of Early Endosome Antigen 1 Is Required for Both
Phosphatidylinositol 3-Phosphate and Rab5 Binding
CRITICAL ROLE OF THIS DUAL INTERACTION FOR ENDOSOMAL
LOCALIZATION*
§,§,
Cell Biology and ¶ Biochemistry and Molecular
Biology, University of Massachusetts Medical School,
Worcester, Massachusetts 01605
*
This work was supported by National Institutes of Health
Grant DK54479 (to S. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell
Biology, University of Massachusetts Medical School, 373 Plantation St., Worcester, MA 01605. Tel.: (508) 856-6898; Fax: (508) 856-1617; E-mail: silvia.corvera@umassmed.edu.
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J.-M. Gaullier, E. Ronning, D. J. Gillooly, and H. Stenmark Interaction of the EEA1 FYVE Finger with Phosphatidylinositol 3-Phosphate and Early Endosomes. ROLE OF CONSERVED RESIDUES J. Biol. Chem., August 4, 2000; 275(32): 24595 - 24600. [Abstract] [Full Text] [PDF]
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M. Cormont, M. Mari, A. Galmiche, P. Hofman, and Y. Le Marchand-Brustel A FYVE-finger-containing protein, Rabip4, is a Rab4 effector involved in early endosomal traffic PNAS, February 13, 2001; 98(4): 1637 - 1642. [Abstract] [Full Text] [PDF]
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J. V. Virbasius, X. Song, D. P. Pomerleau, Y. Zhan, G. W. Zhou, and M. P. Czech Activation of the Akt-related cytokine-independent survival kinase requires interaction of its phox domain with endosomal phosphatidylinositol 3-phosphate PNAS, November 6, 2001; 98(23): 12908 - 12913. [Abstract] [Full Text] [PDF]
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