Abstract
Fragmentation of the mammalian Golgi apparatus during mitosis requires the phosphorylation of a specific subset of Golgi-associated proteins. We have used a biochemical approach to characterize these proteins and report here the identification of golgin-84 as a novel mitotic target. Using cryoelectron microscopy we could localize golgin-84 to the cis-Golgi network and found that it is enriched on tubules emanating from the lateral edges of, and often connecting, Golgi stacks. Golgin-84 binds to active rab1 but not cis-Golgi matrix proteins. Overexpression or depletion of golgin-84 results in fragmentation of the Golgi ribbon. Strikingly, the Golgi ribbon is converted into mini-stacks constituting only approximately 25% of the volume of a normal Golgi apparatus upon golgin-84 depletion. These mini-stacks are able to carry out protein transport, though with reduced efficiency compared with a normal Golgi apparatus. Our results suggest that golgin-84 plays a key role in the assembly and maintenance of the Golgi ribbon in mammalian cells.
Original language | English |
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Pages (from-to) | 201-12 |
Number of pages | 12 |
Journal | Journal of Cell Biology |
Volume | 160 |
Issue number | 2 |
DOIs | |
Publication status | Published - 20 Jan 2003 |
Keywords
- Animals
- Autoantigens
- Endoplasmic Reticulum
- Eukaryotic Cells
- Gene Expression Regulation
- Golgi Apparatus
- HeLa Cells
- Humans
- Intracellular Membranes
- Membrane Proteins
- Microscopy, Electron
- Microtubule Proteins
- Mitosis
- Phosphoproteins
- Protein Transport
- RNA, Small Interfering
- Rats
- Recombinant Fusion Proteins
- Subcellular Fractions
- Viral Proteins
- rab1 GTP-Binding Proteins