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J. Cell Biol., Volume 146, Number 2, January 1, 1999 345-360
Copyright © 1999 by The Rockefeller University Press.

Chimeric Forms of Furin and TGN38 Are Transported from the Plasma Membrane to the Trans-Golgi Network via Distinct Endosomal Pathways

William G. Malleta and Frederick R. Maxfielda
a Department of Biochemistry, Weill Medical College of Cornell University, New York, New York 10021

Correspondence to: Frederick R. Maxfield, Department of Biochemistry, Weill Medical College of Cornell University, 1300 York Ave., Room E-215, New York, NY 10021., frmaxfie{at}mail.med.cornell.edu (E-mail), (212) 746-6405 (phone), (212) 746-8875 (fax)

Furin and TGN38 are membrane proteins that cycle between the plasma membrane and the trans-Golgi network (TGN), each maintaining a predominant distribution in the TGN. We have used chimeric proteins with an extracellular Tac domain and the cytoplasmic domain of TGN38 or furin to study the trafficking of these proteins in endosomes. Previously, we demonstrated that the postendocytic trafficking of Tac-TGN38 to the TGN is via the endocytic recycling pathway (Ghosh, R.N., W.G. Mallet, T.T. Soe, T.E. McGraw, and F.R. Maxfield. 1998. J. Cell Biol. 142:923–936). Here we show that internalized Tac-furin is delivered to the TGN through late endosomes, bypassing the endocytic recycling compartment. The transport of Tac-furin from late endosomes to the TGN appears to proceed via an efficient, single-pass mechanism. Delivery of Tac-furin but not Tac-TGN38 to the TGN is blocked by nocodazole, and the two pathways are also differentially affected by wortmannin. These studies demonstrate the existence of two independent pathways for endosomal transport of proteins to the TGN from the plasma membrane.

Key Words: endocytosis, endosomes, Golgi complex, protease, transport


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