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PMID:18635803
| Citation |
Tu, L, Tai, WC, Chen, L and Banfield, DK (2008) Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 321:404-7 |
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| Abstract |
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. |
| Links |
PubMed Online version:10.1126/science.1159411 |
| Keywords |
Amino Acid Motifs; Amino Acid Sequence; COP-Coated Vesicles/metabolism; Carrier Proteins/metabolism; Coat Protein Complex I/metabolism; Endoplasmic Reticulum/metabolism; Glycosyltransferases/chemistry; Glycosyltransferases/metabolism; Golgi Apparatus/metabolism; Molecular Sequence Data; Protein Transport; Recombinant Fusion Proteins/metabolism; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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See also
References
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