Abstract
The conserved oligomeric Golgi (COG) complex is a soluble hetero-octamer associated with the cytoplasmic surface of the Golgi. Mammalian somatic cell mutants lacking the Cog1 (ldlB) or Cog2 (ldlC) subunits exhibit pleiotropic defects in Golgi-associated glycoprotein and glycolipid processing that suggest COG is involved in the localization, transport, and/or function of multiple Golgi processing proteins. We have identified a set of COG-sensitive, integral membrane Golgi proteins called GEARs (mannosidase II, GOS-28, GS15, GPP130, CASP, giantin, and golgin-84) whose abundances were reduced in the mutant cells and, in some cases, increased in COG-overexpressing cells. In the mutants, some GEARs were abnormally localized in the endoplasmic reticulum and were degraded by proteasomes. The distributions of the GEARs were altered by small interfering RNA depletion of epsilon-COP in wild-type cells under conditions in which COG-insensitive proteins were unaffected. Furthermore, synthetic phenotypes arose in mutants deficient in both epsilon-COP and either Cog1 or Cog2. COG and COPI may work in concert to ensure the proper retention or retrieval of a subset of proteins in the Golgi, and COG helps prevent the endoplasmic reticulum accumulation and degradation of some GEARs.
| Original language | English |
|---|---|
| Pages (from-to) | 2423-35 |
| Number of pages | 13 |
| Journal | Molecular Biology of the Cell |
| Volume | 15 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2004 |
Keywords
- Acetylcysteine
- Animals
- CHO Cells
- Coat Protein Complex I
- Cricetinae
- Cricetulus
- Electrophoretic Mobility Shift Assay
- Endoplasmic Reticulum
- Golgi Apparatus
- Immunoprecipitation
- Intracellular Membranes
- Membrane Proteins
- Microscopy, Fluorescence
- Multiprotein Complexes
- Mutation
- Proteasome Endopeptidase Complex
- Protein Binding
- Protein Transport
- RNA Interference
- SNARE Proteins
- Vesicular Transport Proteins