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- W2028668571 abstract "The information that might help distinguish how the sub-apical compartment relates to apical recycling endosomes includes whether it carries other endosomal markers. One such marker, normally associated with early endosomes, is EEA1. This is a Ptdins(3)P-binding protein involved in regulating endosomal traffic (for a review, see 1 Corvera S. Czech M.P. Trends Cell Biol. 1998; 8: 442-446 Abstract Full Text Full Text PDF PubMed Scopus (183) Google Scholar ). Previous experiments have shown that EEA1 and Rab5 interact, possibly directly, and thus suggested mechanisms of action in which EEA1 binding to both Rab5 and PtdIns(3)P is required for endosomal fusion. In a recent paper in Nature, Christoforidis et al. examined the minimal requirements for endosome–endosome fusion in vitro and found that EEA1 is in fact the only factor needed for minimal fusion activity 2 Christoforidis S. et al. Nature. 1999; 397: 621-625 Crossref PubMed Scopus (654) Google Scholar . Rab5 and other Rab5 effectors appear to act upstream. This leads to a model in which Rab5 is activated on the endosomal membrane by other effectors and then, in combination with PtdIns 3-kinase, targets EEA1 to the membrane. This in turn mediates endosome–endosome docking and fusion, presumably in conjunction with other membrane proteins, such as SNAREs. This paper therefore provides further characterization of the function of EEA1 and highlights it as the first example of a Rab effector acting as a ‘tethering’ protein." @default.
- W2028668571 created "2016-06-24" @default.
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- W2028668571 date "1999-04-01" @default.
- W2028668571 modified "2023-09-26" @default.
- W2028668571 title "The SAC, EEA1, Rab5 and endosome fusion" @default.
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- W2028668571 doi "https://doi.org/10.1016/s0962-8924(99)01543-3" @default.
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