Figure: The CRL5(ASB11) complex mediates ubiquitination and degradation of DIRAS2 (Human).¶
This diagram illustrates how the CRL5(ASB11) E3 ubiquitin ligase complex mediates the ubiquitination and degradation of DIRAS2 in human cells. DIRAS2 is a small GTPase located at the plasma membrane, where it functions in signal transduction pathways. The CRL5 E3 ligase complex consists of CUL5 (cullin-5), which acts as a scaffold, ASB11 (ankyrin repeat and SOCS box containing 11), which functions as the substrate recognition adaptor, and RNF7 (RING-box protein 2), which possesses the E3 ligase activity. ASB11 specifically recognizes and binds to DIRAS2, positioning it for K11-linked polyubiquitination by the CRL5 complex. The ubiquitinated DIRAS2 is subsequently targeted for degradation by the proteasome, resulting in downregulation of DIRAS2-mediated signaling.
Feedback from AI on figure:
{"feedback":"The diagram effectively illustrates the CRL5(ASB11) complex mediating ubiquitination and degradation of DIRAS2. It uses appropriate colors and shapes to distinguish different protein components, with clear labels identifying each element. The pathway flow is logical and easy to follow, showing substrate recognition, ubiquitination, and subsequent degradation. The inclusion of a legend helps readers identify key components quickly. The text is readable and the overall presentation is suitable for publication in scientific journals like Cell or Nature.","necessary_changes":null,"optional_changes":null}