Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

Regulated Protein Degradation

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...

Regulated Protein Degradation

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...

Interactions Between Signaling Pathways

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...

Covalently Linked Protein Regulators

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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Measurement of the ratios of branching fractions and.

Physical review letters·2006

Same author

Direct search for Dirac magnetic monopoles in pp collisions at square root s = 1.96 TeV.

Physical review letters·2006

Same author

Measurement of bottom-quark hadron masses in exclusive J/psi decays with the CDF detector.

Physical review letters·2006

Same author

Measurement of the tt production cross section in pp collisions at square root s = 1.96 TeV using missing E(T) + jets events with secondary vertex b tagging.

Physical review letters·2006

Same author

Preventing renal ischemia-reperfusion injury using small interfering RNA by targeting complement 3 gene.

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons·2006

Same author

Top-quark mass measurement from dilepton events at CDF II.

Physical review letters·2006

Search research articles

Related Experiment Video

Updated: Jun 25, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Crosstalk between the SUMO and ubiquitin pathways.

T Hunter¹, H Sun

¹Molecular and Cell Biology Laboratory, The Salk Institute, 10010 North Torrey Pines Road, La Jolla, CA 920137-1099, USA. hunter@salk.edu

Ernst Schering Foundation Symposium Proceedings

|February 10, 2009

Summary

SUMOylation and ubiquitination pathways communicate through crosstalk. RNF4 E3 ubiquitin ligases specifically target SUMOylated proteins for ubiquitination, revealing a key regulatory mechanism.

Area of Science:

Molecular Biology
Cellular Biology
Biochemistry

Background:

The SUMO (Small Ubiquitin-like Modifier) and ubiquitin pathways are crucial post-translational modification systems.
These pathways regulate diverse cellular processes, including gene expression, DNA repair, and protein stability.
Recent discoveries highlight intricate crosstalk mechanisms between SUMOylation and ubiquitination.

Purpose of the Study:

To review the principles of crosstalk between SUMOylation and ubiquitination.
To focus on the role of the RNF4 family of RING finger E3 ubiquitin ligases in mediating this crosstalk.
To elucidate how SUMOylation status influences protein ubiquitination.

Main Methods:

Literature review of recent findings on SUMO-ubiquitin crosstalk.

More Related Videos

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Related Experiment Videos

Last Updated: Jun 25, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Analysis of the molecular mechanisms employed by RNF4 E3 ubiquitin ligases.

Examination of protein interaction studies and functional assays.

Main Results:

SUMOylation and ubiquitination pathways exhibit significant crosstalk.
RNF4 E3 ubiquitin ligases act as key mediators, specifically recognizing SUMOylated substrates.
This recognition facilitates the subsequent ubiquitination of SUMOylated proteins.

Conclusions:

The RNF4 family of E3 ligases provides a direct link between SUMOylation and ubiquitination.
This crosstalk mechanism is critical for regulating protein fate and cellular functions.
Understanding this interplay offers insights into novel therapeutic strategies.