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.
Tu
Linna
L
Department of Biology, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, Special Administrative Region (SAR) of the People's Republic of China.
Tai
William C S
WC
Chen
Lu
L
Banfield
David K
DK
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D022181:COP-Coated Vesicles / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism*; D020755:Coat Protein Complex I / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D016695:Glycosyltransferases / Q000737:chemistry / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D008969:Molecular Sequence Data; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
D002352:Carrier Proteins; D020755:Coat Protein Complex I; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; C528905:Vps74 protein, S cerevisiae; D016695:Glycosyltransferases