Coronaviruses hijack Golgi apparatus derived COPI vesicles as a membrane source for viral DMV biogenesis
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
zhaohuan Wang
LAB HEAD: Deyin Guo
PROVIDER: PXD070415 | Pride | 2026-06-15
REPOSITORIES: Pride
Dataset's files
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| Treatment1.raw | Raw | |||
| Treatment2.raw | Raw | |||
| checksum.txt | Txt | |||
| control1.raw | Raw | |||
| control2.raw | Raw |
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Project description:Cellular senescence is characterized by persistent cell cycle arrest, apoptosis resistance, and widespread changes in gene expression. Although the functional alterations in organelles like mitochondria and lysosomes are well characterized, senescence-associated changes in the structure and function of the Golgi apparatus remain poorly understood. The Golgi apparatus orchestrates intracellular transport processes that rely heavily on the coating of vesicles with Coatomer Protein Complex I (COPI) proteins (COPA, COPB1, COPB2, COPD, COPE, COPG1, and COPZ1). Based on an earlier RNA interference (RNAi) screen showing that silencing COPI subunits reduced extracellular vesicle (EV) uptake in human diploid WI-38 fibroblasts, and that EV uptake was diminished in senescent WI-38 cells, we sought to functionally analyze COPI proteins in senescent cells. In proliferating cells, individually silencing COPA, COPB1, COPB2, or COPD induced ATF4 production and disrupted autophagy, apoptosis, and cytokine signaling—hallmarks of impaired Golgi-to-ER transport—while individually silencing COPG1, COPE, or COPZ1 altered extracellular matrix organization and GTPase activity. Silencing of any COPI subunit reduced mitochondrial respiration and EV uptake. Proteomic analysis revealed that individual COPI proteins associate with both Golgi and endosomal components, supporting their role in vesicular trafficking. Importantly, the phenotypic effects observed in proliferating cells were not observed in senescent cells, which appeared refractory to further COPI reduction. Our findings underscore the distinct, multifunctional actions of individual COPI proteins and suggest that they are key factors in the intracellular transport networks that sustain homeostatic responses, which become attenuated during senescence.
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Project description:The Golgi apparatus contains many resident enzymes that must remain in place whilst their substrates flow through on their journey from the endoplasmic reticulum to elsewhere in the cell. COPI-coated vesicles bud from the rims of the Golgi stack to recycle Golgi residents to earlier cisternae. Different enzymes are present in different parts of the stack, and at least one COPI adaptor protein, GOLPH3, has been shown to recruit enzymes into vesicles in a specific part of the stack. We have used proximity biotinylation to identify further components of intra-Golgi transport vesicles and found FAM114A2, an uncharacterised cytosolic protein. Affinity chromatography with FAM114A2, and its paralogue FAM114A1 showed that they bind to numerous Golgi resident proteins, with membrane-proximal basic residues in the cytoplasmic tail being sufficient for the interaction. Deletion of both proteins from U2OS cells did not result in substantial defects in Golgi function. However, a Drosophila orthologue of these proteins (CG9590/FAM114A) is also localised to the Golgi and binds directly to COPI. Generation of Drosophila mutants lacking FAM114A revealed defects in glycosylation of glue proteins in the salivary gland. Thus, the FAM114A proteins are COPI vesicle resident proteins that bind to Golgi enzymes and so are candidate adaptors to contribute specificity to COPI vesicle recycling in the Golgi stack.
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Project description:The Golgi apparatus contains many resident enzymes that must remain in place whilst their substrates flow through on their journey from the endoplasmic reticulum to elsewhere in the cell. COPI-coated vesicles bud from the rims of the Golgi stack to recycle Golgi residents to earlier cisternae. Different enzymes are present in different parts of the stack, and at least one COPI adaptor protein, GOLPH3, has been shown to recruit enzymes into vesicles in a specific part of the stack. We have used proximity biotinylation to identify further components of intra-Golgi transport vesicles and found FAM114A2, an uncharacterised cytosolic protein. Affinity chromatography with FAM114A2, and its paralogue FAM114A1 showed that they bind to numerous Golgi resident proteins, with membrane-proximal basic residues in the cytoplasmic tail being sufficient for the interaction. Deletion of both proteins from U2OS cells did not result in substantial defects in Golgi function. However, a Drosophila orthologue of these proteins (CG9590/FAM114A) is also localised to the Golgi and binds directly to COPI. Generation of Drosophila mutants lacking FAM114A revealed defects in glycosylation of glue proteins in the salivary gland. Thus, the FAM114A proteins are COPI vesicle resident proteins that bind to Golgi enzymes and so are candidate adaptors to contribute specificity to COPI vesicle recycling in the Golgi stack.
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Project description:The Golgi apparatus contains many resident enzymes that must remain in place whilst their substrates flow through on their journey from the endoplasmic reticulum to elsewhere in the cell. COPI-coated vesicles bud from the rims of the Golgi stack to recycle Golgi residents to earlier cisternae. Different enzymes are present in different parts of the stack, and at least one COPI adaptor protein, GOLPH3, has been shown to recruit enzymes into vesicles in a specific part of the stack. We have used proximity biotinylation to identify further components of intra-Golgi transport vesicles and found FAM114A2, an uncharacterised cytosolic protein. Affinity chromatography with FAM114A2, and its paralogue FAM114A1 showed that they bind to numerous Golgi resident proteins, with membrane-proximal basic residues in the cytoplasmic tail being sufficient for the interaction. Deletion of both proteins from U2OS cells did not result in substantial defects in Golgi function. However, a Drosophila orthologue of these proteins (CG9590/FAM114A) is also localised to the Golgi and binds directly to COPI. Generation of Drosophila mutants lacking FAM114A revealed defects in glycosylation of glue proteins in the salivary gland. Thus, the FAM114A proteins are COPI vesicle resident proteins that bind to Golgi enzymes and so are candidate adaptors to contribute specificity to COPI vesicle recycling in the Golgi stack.
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