HECT E3s feature the C-terminal HECT domain, which assumes a bilobal architecture, with the N-terminal lobe containing the E2-binding domain and the C-terminal lobe harboring the catalytic cysteine ...

Recent evidence suggests that parts of the ubiquitin-proteasome system are involved in regulating gene expression. Ubiquitylation controls factors such as transcriptional activators, coactivators, and ...

Researchers at TMIMS have revealed that PINK1 (a serine/threonine kinase) and Parkin (a ubiquitin ligating enzyme: E3) work together to ubiquitylate the outer membrane proteins of damaged mitochondria ...

When proteins within the body get tagged with a molecule called ubiquitin, they are essentially marked for destruction. But they can be saved; a deubiquitinase enzyme can remove the ubiquitin, keeping ...

Ubiquitin is the most widely recognised post-translation modifier that bonds to proteins, marking them for degradation in the proteasome. However, there are many other proteins that have similar ...

The COP9 signalosome (CSN) is an evolutionarily conserved multiprotein complex that mediates the repression of photomorphogenesis in the dark in Arabidopsis through the degradation of transcription ...

The Journal of Cell Biology (JCB) is a not-for-profit publication, edited by scientists, and a leading life sciences journal. The JCB publishes papers on all aspects of cellular structure and function ...

Understanding its role has enabled Tansey and colleagues to more comprehensively grasp how ubiquitin functions. They have discovered that Asr1 "glues" ubiquitin on to specific spots in the DNA-copying ...