Tag: Ubiquitin

AUX/IAA proteins are key transcriptional repressors in the auxin signaling pathway. Discover how TIR1 and AFB receptors promote AUX/IAA degradation, release ARF transcription factors, and regulate gene expression involved in roots, shoots, organ formation, phototropism, and plant development.

Degrons are protein degradation signals that determine when proteins are recognized and removed by cellular degradation pathways. Learn how degrons regulate protein stability, signaling, proteostasis and the ubiquitin–proteasome system.

RING E3 ligase complexes use adaptor proteins and substrate receptors to coordinate E2 recruitment, substrate recognition, ubiquitin transfer, cellular localization, and pathway-specific regulation.

RING E3 ligase oligomerization enables the formation of dimers, multimers, and higher-order complexes that regulate E2 recruitment, substrate recognition, ubiquitin transfer, autoubiquitination, and cellular signaling.

RING E3 ligase autoubiquitination provides an important mechanism for regulating E3 stability, activity, localization, and protein turnover through dynamic ubiquitin signaling.

Ubiquitin chain formation by RING E3 ligases generates diverse molecular signals that regulate protein degradation, cellular signaling, DNA damage responses, immunity, and protein homeostasis.

The RING-E2 interaction is central to RING E3 ligase activity. Explore how RING domains bind E2 enzymes, position ubiquitin, and promote transfer to target proteins.

Glycine and post-translational modification are connected through protein structure, sequence context, ubiquitination, protein regulation, proteomics, genetic variation, and cellular signaling.

Protein ubiquitination is a fundamental post-translational modification that regulates protein degradation, cellular signaling, DNA repair, autophagy, protein trafficking and cellular homeostasis.

Timely protein degradation is essential for orderly cell-cycle progression. Explore key cell-cycle regulators, their degradation mechanisms, and how their turnover controls G1/S transition, mitosis, chromosome segregation and mitotic exit.

Protein degradation is a vital cellular process that removes damaged or unnecessary proteins to maintain homeostasis. This article explains the ubiquitin–proteasome system, autophagy, and their roles in cellular regulation and disease.

E3 ubiquitin ligases are key regulators of protein ubiquitination and cellular protein homeostasis. They provide substrate specificity within the ubiquitin system and regulate protein degradation, cell-cycle progression, DNA repair, immune signalling, apoptosis, and other essential cellular processes.