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A more recent version of this article appeared on April 1, 2003
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Submitted on July 15, 2002
Revised on October 22, 2002
Accepted on December 4, 2002
1 Cell Biology and Metabolism Branch National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
2 Division of Tumor Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands
3 Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
* Corresponding author. E-mail address: juan{at}helix.nih.gov.
Sorting of transmembrane proteins and their ligands at various compartments of the endocytic and secretory pathways is mediated by selective incorporation into clathrin-coated intermediates. Previous morphological and biochemical studies have shown that these clathrin-coated intermediates consist of spherical vesicles with a diameter of 60-100 nm. Here we report the use of fluorescent imaging of live cells to demonstrate the existence of a different type of transport intermediate containing associated clathrin coats. Clathrin and the adaptors GGA1 and AP-1, labeled with different spectral variants of the green fluorescent protein, are shown to co-localize to the trans-Golgi network and to a population of vesicles and tubules budding from it. These intermediates are highly pleiomorphic and move towards to peripheral cytoplasm for distances of up to 10 µm with average speeds of ~1 µm/s. The labeled clathrin and GGA1 cycle on and off membranes with half-times of 10-20 s, independently of vesicle budding. Our observations suggest the existence of a novel type of TGN-derived carrier containing associated clathrin, GGA1 and AP-1 that are larger than conventional clathrin-coated vesicles, and that undergo long-range translocation in the cytoplasm before losing their coats.
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