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A more recent version of this article appeared on January 1, 2002
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Submitted on May 7, 2001
Revised on September 27, 2001
Accepted on October 17, 2001
1 Department of Biochemistry, Weill Medical College of Cornell University, New York
2 Departments of Pathology and Anatomy and Cell Biology, Columbia University, College of Physicians and Surgeons, New York
* Corresponding author. E-mail address: frmaxfie{at}mail.med.cornell.edu.
A significant fraction of internalized transferrin (Tf) concentrates in the endocytic recycling compartment (ERC) which is near the microtubule organizing center in many cell types. Tf then recycles back to the cell surface. The mechanisms controlling the localization, morphology and function of the ERC are not fully understood. We examined the relationship of Tf trafficking with microtubules (MTs), specifically the subset of stable, detyrosinated Glu MTs. We found some correlation between the level of stable Glu MTs and the distribution of the ERC; in cells with low levels of Glu MTs concentrated near to the centriole, the ERC was often tightly clustered, whereas in cells with higher levels of Glu MTs throughout the cell, the ERC was more dispersed. The clustered ERC in CHO cells became dispersed when the level of Glu MTs was increased with taxol treatment. Furthermore, in a temperature-sensitive CHO cell line (B104-5), the cells had more Glu MTs when the ERC became dispersed at elevated temperature. Microinjecting purified anti-Glu tubulin antibody into B104-5 cells at elevated temperature induced the redistribution of the ERC to a tight cluster. Microinjection of anti-Glu tubulin antibody slowed recycling of Tf to the cell surface without affecting Tf internalization or delivery to the ERC. Similar inhibition of Tf recycling was caused by microinjecting anti-kinesin antibody. These results suggest that stable Glu MTs and kinesin play a role in the organization of the ERC and in facilitating movement of vesicles from the ERC to the cell surface.
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