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J. Biol. Chem., Vol. 276, Issue 29, 27237-27245, July 20, 2001

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Transforming Growth Factor (TGF)-1 Internalization
MODULATION BY LIGAND INTERACTION WITH TGF- RECEPTORS TYPES I AND II AND A MECHANISM THAT IS DISTINCT FROM CLATHRIN-MEDIATED ENDOCYTOSIS^*

John C. Zwaagstra^§, Mohamed El-Alfy^¶, and Maureen D. O'Connor-McCourt

From the  Cell Surface Recognition Group, Biotechnology Research Institute, National Research Council Canada, Montreal, Quebec H4P 2R2 and the ^¶ Centre de Recherch, Laboratory of Molecular Endocrinology, Sainte-Foy, Quebec G1V 4G2, Canada

Transforming growth factor- (TGF-) internalization was studied by monitoring the uptake of ¹²⁵I-TGF-1 in Mv1Lu cells, which endogenously express TGF- receptors types I (RI), II (RII), and III (RIII), and 293 cells transfected with RI and RII. At 37 °C internalization occurred rapidly, within 10 min of ligand addition. Internalization was optimal in 293 cells expressing both RI and RII. Internalization was prevented by phenylarsine oxide, a nonspecific inhibitor of receptor internalization, but was not affected by reagents that interfere with clathrin-mediated endocytosis such as monodansylcadaverine, K44A dynamin, and inhibitors of endosomal acidification. Electron microscopic examination of Mv1Lu cells treated with ¹²⁵I- TGF-1 at 37 °C indicated that internalization occurred via a noncoated vesicular mechanism. Internalization was prevented by prebinding cells with TGF-1 at 4 °C for 2 h prior to switching the cells to 37 °C. This was attributed to a loss of receptor binding, as indicated by a rapid decrease in the amount of TGF-1 bound to the cell surface at 37 °C and by a reduction in the labeling intensities of RI and RII in ¹²⁵I-TGF-1-cross-linking experiments. Mv1Lu or 293 (RI+RII) cells, prebound with TGF-1 at 4 °C and subsequently stripped of ligand by an acid wash, nevertheless initiated a signaling response upon transfer to 37 °C, suggesting that prebinding promotes formation of stable RI·RII complexes that can signal independently of ligand.

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