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J. Biol. Chem., Vol. 268, Issue 24, 18390-18397, 08, 1993
M Jin and MD Snider
Transferrin receptor (TfR) follows complex pathways of transport after
endocytosis from the cell surface. Most TfR is transported to endosomes and
returns rapidly to the cell surface. In addition, approximately 10% of the
internalized receptor recycles through the Golgi complex. To examine the
role of microtubules in TfR traffic, K562 cultured human leukemia cells
treated with nocodazole to depolymerize microtubules were studied.
Nocodazole caused a 50% increase in the level of surface TfR, which was due
to a change in receptor dynamics. The endocytosis rate in treated cells was
20% of control, indicating that TfR endocytosis via clathrin-coated
vesicles was slowed, whereas the recycling of internalized receptors to the
cell surface was unaffected. In contrast, nocodazole had little effect on
the transport of TfR from the cell surface to the Golgi complex. Thus, the
fragmentation and dispersal of the Golgi complex caused by microtubule
depolymerization, which does not interrupt secretory traffic through this
organelle, also does not block recycling through the Golgi. The decreased
TfR endocytosis via coated vesicles and the increased TfR transport to the
Golgi caused by nocodazole suggest that either (i) endocytosis via coated
vesicles is not the rate-limiting step in transport to the Golgi or (ii)
coated vesicles are not a part of this pathway. Finally, because nocodazole
inhibits traffic from endosomes to lysosomes, surface-to-Golgi transport
probably does not involve a lysosomal intermediate.
Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex
Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4935.
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