Different roles of COPI proteins reduced during cell aging

Silencing subunits of the coatomer protein I (COPI) complex reduced extracellular vesicle uptake in proliferating WI-38 fibroblasts.

• Silencing COPI constituents COPA, COPB1, COPB2, or COPD led to increased production of ATF4 and disrupted key cellular processes such as autophagy, apoptosis, and cytokine signaling.
• These disruptions are associated with impaired transport mechanisms between the Golgi and endoplasmic reticulum.
• Silencing other COPI constituents, including COPG1, COPE, or COPZ1, affected the production of extracellular matrix proteins.
• Individual COPI proteins were found to associate with Golgi and endosomal proteins, indicating their involvement in vesicular trafficking.
• In senescent WI-38 fibroblasts, silencing COPI proteins did not produce the same effects observed in proliferating cells.

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