Figure: TRIM27-mediated ubiquitination and degradation of TBK1 (Human)¶
This figure illustrates the TRIM27-mediated ubiquitination and degradation of TBK1 in human cells, which regulates type I interferon production. The pathway begins at the plasma membrane where SIGLEC1 binds to extracellular virions. This triggers activation of TYROBP, another membrane protein, which subsequently activates the cytoplasmic adaptor protein PTPN11. PTPN11 then activates TRIM27, an E3 ubiquitin ligase. TRIM27 ubiquitinates TBK1 (TANK-binding kinase 1), targeting it for degradation. When TBK1 is degraded, its normal function of positively regulating type I interferon production is inhibited, resulting in negative regulation of the interferon response. Blue arrows indicate activation, while red dashed arrows indicate inhibition. The pathway illustrates how viral recognition at the cell membrane can lead to downregulation of the inflammatory interferon response through a precisely coordinated series of protein-protein interactions.
Feedback from AI on figure:
{"feedback":"The final diagram effectively illustrates the TRIM27-mediated ubiquitination and degradation of TBK1 pathway with excellent clarity and scientific accuracy. The key strengths include clear spatial organization showing distinct cellular compartments, well-chosen color scheme differentiating between membrane and cytoplasmic proteins, improved use of colored and styled arrows to distinguish activation from inhibition, comprehensive legend, clear labeling of protein components and their interactions, and professional presentation style appropriate for scientific journals like Cell or Nature.","necessary_changes":null,"optional_changes":null}