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J Biol Chem, Vol. 274, Issue 51, 36107-36116, December 17, 1999

The Cytoplasmic, Transmembrane, and Stem Regions of Glycosyltransferases Specify Their in Vivo Functional Sublocalization and Stability in the Golgi*

Eckart GrabenhorstDagger and Harald S. Conradt

From the Protein Glycosylation Group, Gesellschaft für Biotechnologische Forschung mbH, Mascheroder Weg 1, D-38124 Braunschweig, Germany

We provide evidence for the presence of targeting signals in the cytoplasmic, transmembrane, and stem (CTS) regions of Golgi glycosyltransferases that mediate sorting of their intracellular catalytic activity into different functional subcompartmental areas of the Golgi. We have constructed chimeras of human alpha 1,3-fucosyltransferase VI (FT6) by replacement of its CTS region with those of late and early acting Golgi glycosyltransferases and have stably coexpressed these constructs in BHK-21 cells together with the secretory reporter glycoprotein human beta -trace protein. The sialyl Lewis X:Lewis X ratios detected in beta -trace protein indicate that the CTS regions of the early acting GlcNAc-transferases I (GnT-I) and III (GnT-III) specify backward targeting of the FT6 catalytic domain, whereas the CTS region of the late acting human alpha 1,3-fucosyltransferase VII (FT7) causes forward targeting of the FT6 in vivo activity in the biosynthetic glycosylation pathway. The analysis of the in vivo functional activity of nine different CTS chimeras toward beta -trace protein allowed for a mapping of the CTS donor glycosyltransferases within the Golgi/trans-Golgi network: GnT-I < (ST6Gal I, ST3Gal III) < GnT-III < ST8Sia IV < GalT-I < (FT3, FT6) < ST3Gal IV < FT7. The sensitivity or resistance of the donor glycosyltransferases toward intracellular proteolysis is transferred to the chimeric enzymes together with their CTS regions. Apparently, there are at least three different signals contained in the CTS regions of glycosyltransferases mediating: first, their Golgi retention; second, their targeting to specific in vivo functional areas; and third, their susceptibility toward intracellular proteolysis as a tool for the regulation of the intracellular turnover.

* This work was supported in part by European Union Grant BIO2-CT94-3069 (to H. S. C.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ245699, AJ245700, and AJ245701.

Dagger To whom correspondence should be addressed: Protein Glycosylation Group, GBF- Gesellschaft für Biotechnologische Forschung mbH, Mascheroder Weg 1, D-38124 Braunschweig, Germany. Tel.: 49-531-6181-219; Fax: 49-531-6181-202; E-mail: egr@gbf.de.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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