Figure: Mumps-V inhibition of STAT3 via DDB1/CUL4A (Human-Paramyxovirus)¶
This figure illustrates the molecular mechanism by which Mumps virus inhibits STAT3 signaling in human cells. The viral P/V protein (P33483) acts as a molecular adaptor (GO:0060090), triggering suppression of the host JAK-STAT signaling cascade (GO:0039564). It interacts with host DNA Damage Binding Protein 1 (DDB1, Q16531), which has cullin family protein binding activity (GO:0097602). DDB1 recruits Cullin-4A (CUL4A, Q13619) to form a ubiquitin ligase complex with RING-box protein 1 (RBX1, P62877). This E3 ubiquitin ligase complex (GO:0061630) marks STAT3 (P40763) for degradation, inhibiting its DNA-binding transcription factor activity (GO:0000981) in the nucleus, thereby disrupting cytokine-mediated signaling (GO:0019221).
Feedback from AI on figure:
{"feedback":"The diagram effectively illustrates the pathway through which Mumps virus inhibits STAT3 signaling via the DDB1/CUL4A complex. The cellular compartments are clearly delineated, with the nucleus and cytoplasm properly labeled. The pathway components are well-organized, with viral and host proteins distinguished by different colors, and the interactions between them clearly marked with appropriate arrows and text labels. The GO terms are included at a readable size, providing functional context for each interaction. The addition of ubiquitin tags as an implicit detail enhances understanding of the mechanism without misrepresenting the source data. The inhibitory relationship is highlighted with a distinct red dashed arrow, making the key regulatory effect immediately apparent. The comprehensive legend supports interpretation of all visual elements.","necessary_changes":null,"optional_changes":null}