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Glycobiology Advance Access published online on June 2, 2005
Glycobiology, doi:10.1093/glycob/cwi085
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Received November 12, 2004
Revised May 20, 2005
Accepted May 23, 2005

Article

ER retention of the large splice variant of the UDP-galactose transporter is caused by a di-lysine motif

Roland Kabuß 1, Angel Ashikov 1, Stefan Oelmann 1, Rita Gerardy-Schahn 1*, and Hans Bakker 1

1 Zelluläre Chemie, Zentrum Biochemie, Medizinische Hochschule Hannover, Carl-Neuberg-Str. 1, 30625 Hannover, Germany

* To whom correspondence should be addressed.
Rita Gerardy-Schahn, E-mail: gerardy-schahn.rita{at}mh-hannover.de


  Abstract

Nucleotide-sugar transporters supply mainly the Golgi glycosyltransferases with substrates. Some glycosyltransferases in the ER, however, also use activated sugars. Recent studies have demonstrated that UDP-galactose (UDP-Gal) is the substrate for the ER resident ceramidegalactosyltransferase (cer-GalT) and cells expressing cer-GalT are able to retain the UDP-Gal transporter by physical contacts formed between the two proteins. Here, we describe a second active mechanism for ER localization of the UDP-Gal transporter. The UDP-Gal transporter is produced in two splice forms UGT1 and UGT2. The proteins vary only at their extreme Ctermini but show strikingly different intracellular distribution. While N-terminally epitope tagged forms of UGT1 localize exclusively to the Golgi, similar constructs of UGT2 show both ER and Golgi localization. The di-lysine motif KVKGS contained in UGT2 can be demonstrated to be responsible for the dual localization because: (i) disturbance of the signal via site specific mutation or C-terminal extension completely shifts the transporter to the Golgi, (ii) transfer of the di-lysine motif is sufficient to redistribute the Golgi CMP-sialic acid transporter to the ER and, (iii) replacement of KVKGS by the strong ER retention signal KKNT is sufficient to completely retain UGT2 in the ER.

Keywords: Di-lysine / ER retention / Golgi / Nucleotide sugar transporter / UDP-galactose transporter.
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