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A more recent version of this article appeared on April 1, 2002
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Submitted on October 29, 2001
Revised on January 7, 2002
Accepted on January 14, 2002
1 Department of Cell Biology, University Medical Center Utrecht and Institute of Biomembranes, 3584 CX Utrecht, The Netherlands, and Center for Biomedical Genetics, PO Box 80042, 3508 TA Utrecht, The Netherlands
2 Physiological Laboratory, University of Liverpool, Liverpool L69 3BX, United Kingdom
3 Department of Cell Biology, University Medical Center Utrecht and Institute of Biomembranes, 3584 CX Utrecht, The Netherlands
* Corresponding author. E-mail address: j.klumperman{at}lab.azu.nl.
In many cells endosomal vacuoles show clathrin coats of which the function is unknown. Here we show that this coat is predominantly present on early endosomes (EE) and has a characteristic bi-layered appearance in the electron microscope (EM). By immunoEM we show that the coat contains clathrin heavy as well as light chain, but lacks the adaptor complexes AP1, AP2 and AP3, by which it differs from clathrin coats on endocytic vesicles and recycling endosomes. The coat is insensitive to short incubations with Brefeldin A, but disappears in the presence of the PtdIns3-kinase inhibitor wortmannin. No association of endosomal coated areas with tracks of tubulin or actin was found. By quantitative immunoEM, we found that the lysosomal-targeted receptors for growth hormone (GHR) and epidermal growth factor (EGFR) are concentrated in the coated membrane areas, whereas the recycling transferrin receptor (TfR) is not. In addition, we found that the proteasomal inhibitor MG 132 induces a redistribution of a truncated GHR (GHR-369) towards recycling vesicles, which coincided with a redistribution of endosomal vacuole associated GHR-369 to the non-coated areas of the limiting membrane. Together, these data suggest a role for the bi-layered clathrin coat on vacuolar endosomes in targeting of proteins to lysosomes.
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