Signal-mediated dynamic retention of glycosyltransferases in the Golgi

Linna Tu, William C S TAI, Lu Chen, David K. Banfield

Research output: Contribution to journalJournal articlepeer-review

181 Citations (Scopus)


Golgi-resident glycosyltransferases are a family of enzymes that sequentially modify glycoproteins in a subcompartment-specific manner. These type II integral membrane proteins are characterized by a short cytoplasmically exposed amino-terminal tail and a luminal enzymatic domain. The cytoplasmic tails play a role in the localization of glycosyltransferases, and coat protein complex I (COPI) vesicle-mediated retrograde transport is also involved in their Golgi localization. However, the tails of these enzymes lack known COPI-binding motifs. Here, we found that Vps74p bound to a pentameric motif present in the cytoplasmic tails of the majority of yeast Golgi-localized glycosyltransferases, as well as to COPI. We propose that Vps74p maintains the steady-state localization of Golgi glycosyltransferases dynamically, by promoting their incorporation into COPI-coated vesicles.

Original languageEnglish
Pages (from-to)404-407
Number of pages4
Issue number5887
Publication statusPublished - 18 Jul 2008

Scopus Subject Areas

  • General


Dive into the research topics of 'Signal-mediated dynamic retention of glycosyltransferases in the Golgi'. Together they form a unique fingerprint.

Cite this