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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Related Experiment Video

Updated: May 10, 2026

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Ubiquitin system: direct effects join the signaling.

Alexander L Chernorudskiy1, Murat R Gainullin

  • 1Postgenomic Technology Group, Institute of Applied and Fundamental Medicine, Nizhny Novgorod State Medical Academy, Nizhny Novgorod, 603005, Russia. chalbio@gmail.com

Science Signaling
|June 20, 2013
PubMed
Summary

Ubiquitylation directly impacts protein interactions without needing specific receptors. This posttranslational modification offers a flexible, two-level regulatory mechanism for cellular processes.

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

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Detection of Protein Ubiquitination
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Detection of Protein Ubiquitination

Published on: August 19, 2009

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Last Updated: May 10, 2026

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

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Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Ubiquitylation is a crucial posttranslational modification regulating eukaryotic protein function.
  • Traditionally, ubiquitin's role is understood through specific ubiquitin-binding domains recognizing ubiquitin signals.
  • Emerging evidence points to direct effects of ubiquitylation on protein interactions.

Purpose of the Study:

  • To explore the direct effects of ubiquitylation on protein-protein interactions.
  • To present examples illustrating this direct regulatory mechanism.
  • To propose a novel two-level regulatory model mediated by ubiquitylation.

Main Methods:

  • Literature review and synthesis of existing data.
  • Analysis of case studies demonstrating direct ubiquitylation effects.
  • Conceptual framework development for a two-level regulatory model.

Main Results:

  • Ubiquitin attachment can directly alter protein interactions by causing steric hindrance.
  • These direct effects operate independently of canonical ubiquitin-binding domains.
  • Examples provided support the concept of ubiquitylation influencing protein complex formation.

Conclusions:

  • Ubiquitylation exerts direct regulatory control over protein interactions, expanding beyond receptor-mediated signaling.
  • A dual-level regulatory mechanism involving both direct and indirect effects of ubiquitylation enhances cellular process flexibility.
  • This direct mechanism provides a new perspective on the multifaceted roles of ubiquitylation in cell biology.