Ubiquitin Archives - Laboratory Notes

AUX/IAA Protein

admin — Mon, 28 Sep 2026 23:02:15 +0000

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.

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Degron

admin — Sat, 26 Sep 2026 14:43:46 +0000

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.

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RING E3 Ligase Complexes & Adaptor Proteins

admin — Fri, 25 Sep 2026 11:57:39 +0000

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

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RING E3 Ligase Oligomerization

admin — Fri, 25 Sep 2026 11:48:35 +0000

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.

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RING E3 Ligase Autoubiquitination

admin — Fri, 25 Sep 2026 11:06:51 +0000

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

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Ubiquitin Chain Formation by RING E3 Ligases

admin — Fri, 25 Sep 2026 10:54:34 +0000

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

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RING-E2 Interaction: How RING E3 Ligase Promote Ubiquitin Transfer

admin — Fri, 25 Sep 2026 10:28:18 +0000

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.

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Glycine and Post-Translational Modification

admin — Sun, 20 Sep 2026 14:15:14 +0000

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

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Protein Ubiquitination

admin — Sun, 30 Aug 2026 10:34:07 +0000

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

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Timed Proteolysis as a Molecular Engine of Cell-Cycle Progression: Key Proteins Whose Degradation Drives Cell-Cycle Transitions

admin — Sat, 22 Aug 2026 23:12:32 +0000

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.

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Protein Degradation

admin — Sun, 02 Aug 2026 16:57:52 +0000

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.

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E3 Ubiquitin Ligase

admin — Fri, 22 Aug 2025 17:38:37 +0000

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.

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