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.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Li X,Kaloyanova D,van Eijk M,Eerland R,van der Goot G,Oorschot V,Klumperman J,Lottspeich F,Starkuviene V,Wieland FT,Helms JBdoi
10.1091/mbc.e06-03-0236subject
Has Abstractpub_date
2007-04-01 00:00:00pages
1261-71issue
4eissn
1059-1524issn
1939-4586pii
E06-03-0236journal_volume
18pub_type
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