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J. Biol. Chem., Vol. 277, Issue 15, 12816-12823, April 12, 2002
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From the Graduate Program for Regulation of Biological Signals,
Graduate School of Bioagricultural Sciences, Nagoya University,
Chikusa, Nagoya, 464-8601 Japan
Wnt is a family of cysteine-rich secreted
glycoproteins, which controls the fate and behavior of the cells in
multicellular organisms. In the absence of Drosophila
segment polarity gene porcupine (porc), which
encodes an endoplasmic reticulum (ER) multispanning transmembrane
protein, the N-glycosylation of Wingless (Wg), one of
Drosophila Wnt family, is impaired. In contrast, the
ectopic expression of porc stimulates the
N-glycosylation of both endogenously and exogenously
expressed Wg. The N-glycosylation of Wg in the ER occurs
posttranslationally, while in the presence of dithiothreitol, it
efficiently occurs cotranslationally. Thus, the cotranslational
disulfide bond formation of Wg competes with the
N-glycosylation by an oligosaccharyl transferase
complex. Porc binds the N-terminal 24-amino acid domain (residues
83-106) of Wg, which is highly conserved in the Wnt family and
stimulates the N-glycosylation at surrounding sites. Porc
is also necessary for the processing of Drosophila Wnt-3/5
in both embryos and cultured cells. Thus, Porc binds the N-terminal
specific domain of the Wnt family and stimulates its posttranslational
N-glycosylation by anchoring them at the ER membrane
possibly through acylation.
Drosophila Segment Polarity Gene Product Porcupine
Stimulates the Posttranslational N-Glycosylation of
Wingless in the Endoplasmic Reticulum*
*
This work was supported by a Research Fellowship from the
Japan Society for the Promotion of Science for Young Scientists (to
T. K.) and a Grant-in-Aid for Scientific Research from the Japan
Society for the Promotion of Science (to Y. K. and T. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 81-52-789-5237;
Fax: 81-52-789-5237; E-mail: emi@nuagr1.agr.nagoya-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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