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Updated: Feb 10, 2026

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Published on: September 10, 2020
Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport
Miwa Sohda1, Yoshio Misumi, Akitsugu Yamamoto
1Division of Oral Biochemistry, Niigata University Graduate School of Medical and Dental Sciences, Chuo-ku, Niigata 951-8514, Japan.
Insights
Golgin-84, a Golgi tether, is crucial for intra-Golgi retrograde traffic by interacting with the COG complex. This interaction precedes SNARE assembly, ensuring proper vesicle tethering and Golgi function.
Area of Science:
- Cell Biology
- Molecular Biology
- Golgi Apparatus Function
Background:
- Golgin-84 is a Golgi membrane protein that tethers coat protein I (COPI) vesicles.
- Golgin-84 interacts with the conserved oligomeric Golgi (COG) complex, specifically its Cog7 subunit.
- Intra-Golgi retrograde traffic is essential for maintaining Golgi homeostasis.
Purpose of the Study:
- To investigate the role of golgin-84 as a tether for COPI vesicles in intra-Golgi retrograde traffic.
- To elucidate the functional relationship between golgin-84 and the COG complex in vesicle tethering.
Main Methods:
- Golgin-84 knockdown (KD) in cells.
- Analysis of glycoprotein maturation (CD44, lamp1).
- Golgi morphology and protein localization studies.
- Vesicle analysis for intra-Golgi SNAREs and GPP130.
- COG complex subunit (Cog3, Cog7) KD experiments.
- Investigation of golgin-84 and CASP interactions.
Main Results:
- Golgin-84 KD disrupted glycoprotein maturation and caused Golgi fragmentation.
- Depletion of golgin-84 led to accumulation of vesicles with SNAREs and GPP130.
- Diminishing the COG complex yielded similar results, indicating a strong correlation.
- COG complex-dependent vesicles in Cog3 or Cog7 KD cells contained golgin-84.
- Golgin-84's interaction with CASP decreased in Cog3 KD cells.
Conclusions:
- Golgin-84 functions as a critical tether for COPI vesicles in intra-Golgi retrograde transport.
- The interaction between golgin-84 and the COG complex is vital for vesicle tethering.
- Golgin-84 engages with the COG complex prior to SNARE assembly during retrograde traffic.
Abstract:
The coiled-coil Golgi membrane protein golgin-84 functions as a tethering factor for coat protein I (COPI) vesicles. Protein interaction analyses have revealed that golgin-84 interacts with another tether, the conserved oligomeric Golgi (COG) complex, through its subunit Cog7. Therefore, we explored the function of golgin-84 as the tether for COPI vesicles of intra-Golgi retrograde traffic. First, glycosylic maturation of both plasma membrane (CD44) and lysosomal (lamp1) glycoproteins was distorted in golgin-84 knockdown (KD) cells. The depletion of golgin-84 caused fragmentation of the Golgi with the mislocalization of Golgi resident proteins, resulting in the accumulation of vesicles carrying intra-Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and cis-Golgi membrane protein GPP130. Similar observations were obtained by diminution of the COG complex, suggesting a strong correlation between the two tethers. Indeed, COG complex-dependent (CCD) vesicles that accumulate in Cog3 or Cog7 KD cells carried golgin-84. Surprisingly, the interaction between golgin-84 and another candidate tethering partner CASP (CDP/cut alternatively spliced product) decreased in Cog3 KD cells. These results indicate that golgin-84 on COPI vesicles interact with the COG complex before SNARE assembly, suggesting that the interaction of golgin-84 with COG plays an important role in the tethering process of intra-Golgi retrograde vesicle traffic.
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