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Originally published In Press as doi:10.1074/jbc.M111799200 on January 2, 2002

J. Biol. Chem., Vol. 277, Issue 12, 10374-10378, March 22, 2002
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The Cytoplasmic Tail of alpha 1,3-Galactosyltransferase Inhibits Golgi Localization of the Full-length Enzyme*

Julie MillandDagger , Sarah M. Russell§, Hayley C. DodsonDagger , Ian F. C. McKenzieDagger , and Mauro S. SandrinDagger ||

From the Dagger  John Connell Laboratory for Glycobiology, The Austin Research Institute, Studley Road, Heidelberg 3084, Australia and § The Peter MacCallum Cancer Institute, Smorgon Family Building, St. Andrews Place, East Melbourne 3002, Australia

It is currently under debate whether the mechanism of Golgi retention of different glycosyltransferases is determined by sequences in the transmembrane, luminal, or cytoplasmic domains or a combination of these domains. We have shown that the cytoplasmic domains of alpha 1,3-galactosyltransferase (GT) and alpha 1,2-fucosyltransferase (FT) are involved in Golgi localization. Here we show that the cytoplasmic tails of GT and FT are sufficient to confer specific Golgi localization. Further, we show that the expression of only the cytoplasmic tail of GT can lead to displacement or inhibition of binding of the whole transferase and that cells expressing the cytoplasmic tail of GT were not able to express full-length GT or its product, Galalpha 1,3Gal. Thus, the presence of the cytoplasmic tail prevented the localization and function of full-length GT, suggesting a possible specific Golgi binding site for GT. The effect was not altered by the inclusion of the transmembrane domain. Although the transmembrane domain may act as an anchor, these data show that, for GT, only the cytoplasmic tail is involved in specific localization to the Golgi.

* This work was supported by the Mizutani Foundation for Glycoscience and The National Health and Medical Research Council of Australia.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.

Supported by a Wellcome Senior Research Fellowship in Medical Science in Australia.

|| To whom correspondence should be addressed: The Austin Research Institute, Austin and Repatriation Medical Center, Studley Rd., Heidelberg 3084, Australia. Tel.: 61-3-9287-0666; Fax: 61-3-9287-0604; E-mail, m.sandrin@ari.unimelb.edu.au.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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