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A more recent version of this article appeared on December 1, 2003
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Submitted on June 11, 2003
Revised on August 7, 2003
Accepted on August 21, 2003
1 Institute for Medical Biochemistry, Center for Molecular Biology of Inflammation, von Esmarch-Str. 56, D-48149 Münster, Germany
2 Department of Cell Biology, University Medical Center Utrecht, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands
* Corresponding author. E-mail address: gerke{at}uni-muenster.de.
* Corresponding author. E-mail address: gerke{at}uni-muenster.de.
The Ca2+ and lipid binding protein annexin 2, which resides in a tight heterotetrameric complex with the S100 protein S100A10 (p11), has been implicated in the structural organization and dynamics of endosomal membranes. To elucidate the function of annexin 2 and S100A10 in endosome organization and trafficking, we used RNA-mediated interference (RNAi) to specifically suppress annexin 2 and S100A10 expression. Down-regulation of both proteins perturbed the distribution of transferrin receptor- and rab11-positive recycling endosomes but did not affect uptake into sorting endosomes. The phenotype was highly specific and could be rescued by reexpression of the N-terminal annexin 2 domain or S100A10 in annexin 2- or S100A10-depleted cells, respectively. Whole-mount immunoelectron microscopy of the aberrantly localized recycling endosomes in annexin 2/S100A10 down-regulated cells revealed extensively bent tubules and an increased number of endosome-associated clathrin-positive buds. Despite these morphological alterations the kinetics of transferrin uptake and recycling were not affected to a significant extent indicating that the proper positioning of recycling endosomes is not a rate-limiting step in transferrin recycling. The phenotype generated by this transient loss-of-protein approach shows for the first time that the annexin 2/S100A10 complex functions in the intracellular positioning of recycling endosomes and that both subunits are required for this activity.
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