| Literature DB >> 17251550 |
Xueyi Li1, Dora Kaloyanova, Martin van Eijk, Ruud Eerland, Gisou van der Goot, Viola Oorschot, Judith Klumperman, Friedrich Lottspeich, Vytaute Starkuviene, Felix T Wieland, J Bernd Helms.
Abstract
The Golgi apparatus consists of a series of flattened cisternal membranes that are aligned in parallel to form stacks. Cytosolic-oriented Golgi-associated proteins have been identified that may coordinate or maintain the Golgi architecture. Here, we describe a novel GPI-anchored protein, Golgi-resident GPI-anchored protein (GREG) that has a brefeldin A-sensitive Golgi localization. GREG resides in the Golgi lumen as a cis-oriented homodimer, due to strong interactions between coiled-coil regions in the C termini. Dimerization of GREG as well as its Golgi localization depends on a unique tandem repeat sequence within the coiled-coil region. RNA-mediated interference of GREG expression or expression of GREG mutants reveals an essential role for GREG in maintenance of the Golgi integrity. Under these conditions, secretion of the vesicular stomatitis virus glycoprotein protein as a marker for protein transport along the secretory pathway is inhibited, suggesting a loss of Golgi function as well. These results imply the involvement of a luminal protein in Golgi structure and function.Entities:
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Year: 2007 PMID： 17251550 PMCID： PMC1838991 DOI： 10.1091/mbc.e06-03-0236
Source DB: PubMed Journal: Mol Biol Cell ISSN： 1059-1524 Impact factor: 4.138