Signal-mediated dynamic retention of glycosyltransferases in the Golgi.

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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, COP-Coated Vesicles, Carrier Proteins, Coat Protein Complex I, Endoplasmic Reticulum, Glycosyltransferases, Golgi Apparatus, Molecular Sequence Data, Protein Transport, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Science
Date: Jul. 18, 2008
Download Curated Data For This Publication
85850
Switch View:
  • Interactions 10