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

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....

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...

The Unfolded Protein Response

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

Intralumenal Vesicles and Multivesicular Bodies

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

Receptor Downregulation in MVBs

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...

You might also read

Related Articles

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

Sort by

Same author

Spontaneous Helical Alignment of Smooth Muscle Cells to Form a Medial Layer for Engineered Microvasculature.

Advanced healthcare materials·2026

Same author

The EF-hand domain of MINDY3 is a ubiquitin and RAD23 UBL-binding domain.

EMBO reports·2026

Same author

Piecing together the alveolar-capillary unit: arterial-venous capillary polarization.

American journal of physiology. Lung cellular and molecular physiology·2026

Same author

Variation in <i>SNX29</i> and Acute Vasodilator Response in Pulmonary Arterial Hypertension.

Circulation research·2026

Same author

Structure-Guided Discovery of OAT-4828 as Potent, Selective, and Orally Bioavailable USP7 Inhibitor with <i>In Vivo</i> Antileukemic Activity.

Journal of medicinal chemistry·2026

Same author

Influence of total electron dose on the quality of nucleic acids potential maps in Cryo-EM.

Ultramicroscopy·2026

Search research articles

Related Experiment Video

Updated: Oct 13, 2025

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Urm1, not quite a ubiquitin-like modifier?

Lars Kaduhr¹, Cindy Brachmann¹, Keerthiraju Ethiraju Ravichandran^2,3

¹Universität Kassel, Institut für Biologie, Fachgebiet Mikrobiologie, Heinrich-Plett-Str. 40, 34132 Kassel, Germany.

Microbial Cell (Graz, Austria)

|November 16, 2021

Summary

Ubiquitin related modifier 1 (Urm1) modifies proteins via urmylation, a process influenced by oxidative stress. This study reveals how antioxidant enzyme activity impacts Urm1 conjugation, suggesting a link to cellular defense mechanisms.

Keywords:

Urm1 peroxiredoxin Ahp1 protein urmylation tRNA thiolation yeast

More Related Videos

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Related Experiment Videos

Last Updated: Oct 13, 2025

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Area of Science:

Biochemistry
Molecular Biology
Cellular Biology

Background:

Ubiquitin related modifier 1 (Urm1) is a unique protein in the ubiquitin-fold family, involved in tRNA thiolation and protein modification through urmylation.
Urmylation is linked to oxidative stress and targets antioxidant proteins like 2-Cys peroxiredoxins, but its molecular mechanism and regulation by these targets remained unclear.

Purpose of the Study:

To investigate the molecular mechanisms of Ahp1 (yeast 2-Cys peroxiredoxin) urmylation.
To determine how the activity of antioxidant enzymes affects Urm1 conjugation.
To explore the relationship between Urm1 utilization and cellular oxidant defense.

Main Methods:

In-depth study of Ahp1 urmylation in yeast.
In vivo assays to assess the impact of organic peroxide concentrations on Ahp1 urmylation.

Main Results:

Ahp1 urmylation is influenced by promiscuous lysine target sites and specific redox requirements.
The dimer interface and 2-Cys redox-active centers of Ahp1 are critical for Urm1 conjugation.
High organic peroxide levels inhibit Ahp1 urmylation, indicating a connection between Urm1 conjugation and cellular antioxidant defense.

Conclusions:

Urm1 conjugation is modulated by the redox state and structural features of its target proteins, such as Ahp1.
A potential link exists between Urm1 conjugation and cellular oxidant defense mechanisms.
The findings suggest a re-evaluation of Urm1's role and the nature of urmylation, questioning its strict ubiquitin-like characteristics.