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Papers In Press, published online ahead of print February 7, 2006
Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215
Corresponding Author: rhaltiwanger{at}ms.cc.sunysb.edu
O-fucose is an unusual form of glycosylation found on Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 repeats (TSRs) in many secreted and transmembrane proteins. Recently O-fucose on EGF repeats was shown to play important roles in Notch signaling. In contrast, physiological roles for O-fucose on TSRs are unknown. In the accompanying paper, we demonstrated that an enzyme distinct from protein O-fucosyltransferase 1 adds O-fucose to TSRs. A known homologue of O-fucosyltransferase 1 is a putative protein O-fucosyltransferase 2. The cDNA sequence encoding O-fucosyltransferase 2 was originally identified during a database search for fucosyltransferases in Drosophila. Like O-fucosyltransferase 1, O-fucosyltransferase 2 is conserved from C. elegans to humans. Although O-fucosyltransferase 2 was assumed to be another protein O-fucosyltransferase, no biochemical characterization existed supporting this contention. Here we show that RNAi-mediated reduction of O-fucosyltransferase 2 message significantly decreased TSR specific O-fucosyltransferase activity in Drosophila S2 cells. We also found that O-fucosyltransferase 2 is predominantly localized in the ER compartment of these cells. Furthermore, we expressed recombinant Drosophila O-fucosyltransferase 2 and showed that it O-fucosylates TSRs but not EGF repeats in vitro. These results demonstrate that O-fucosyltransferase 2 is in fact a TSR specific O-fucosyltransferase.
J. Biol. Chem, 10.1074/jbc.M511975200
Submitted on November 7, 2005
Revised on February 7, 2006
Accepted on February 7, 2006
Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats
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