Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Proteasome01:13

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 Proteasome02:18

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 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...
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...
Export of Misfolded Proteins out of the ER01:32

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...
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.

You might also read

Related Articles

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

Sort by
Same author

Catch Me If You Can: How <i>Xylella fastidiosa</i> Thrives in the Xylem.

Annual review of phytopathology·2026
Same author

Biosensors reveal distinct cytosolic pH and redox dynamics across seedlings in response to danger signals and pathogen infection.

Journal of experimental botany·2026
Same author

Dawn of a new era for parasitic plant biology.

Plant & cell physiology·2026
Same author

CLE peptides in plant-biotic interactions.

The New phytologist·2026
Same author

Jasmonic acid signalling is targeted by a smut fungal Tin2-fold effector.

Journal of experimental botany·2025
Same author

Extracellular Vesicles From Xylella fastidiosa Carry sRNAs and Genomic Islands, Suggesting Roles in Recipient Cells.

Journal of extracellular vesicles·2025
Same journal

Malaria Cytoskeletal Proteins Require Alveolin-Alveolin Interactions for Differential Localization: Recruitment and Organization of Alveolin Proteins.

Cellular microbiology·2025
Same journal

Vam6/Vps39/TRAP1-domain proteins influence vacuolar morphology, iron acquisition and virulence in Cryptococcus neoformans.

Cellular microbiology·2021
Same journal

Hepatitis B virus envelope proteins can serve as therapeutic targets embedded in the host cell plasma membrane.

Cellular microbiology·2021
Same journal

Chlamydia and HPV induce centrosome amplification in the host cell through additive mechanisms.

Cellular microbiology·2021
Same journal

Entry of the Varicellovirus Canid herpesvirus 1 into Madin-Darby canine kidney epithelial cells is pH-independent and occurs via a macropinocytosis-like mechanism but without increase in fluid uptake.

Cellular microbiology·2021
Same journal

Dengue virus replication enhances labile zinc pools by modulation of ZIP8.

Cellular microbiology·2021
See all related articles

Related Experiment Video

Updated: Jun 22, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

How microbes utilize host ubiquitination.

Thomas Spallek1, Silke Robatzek, Vera Göhre

  • 1Max-Planck-Institute for Plant Breeding Research, Cologne, Germany.

Cellular Microbiology
|June 16, 2009
PubMed
Summary
This summary is machine-generated.

Pathogenic bacteria hijack host ubiquitination systems to suppress immunity and promote survival. They achieve this mimicry through gene transfer or convergent evolution, gaining crucial ubiquitination functions.

More Related Videos

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

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Related Experiment Videos

Last Updated: Jun 22, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

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

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Area of Science:

  • Molecular Biology
  • Immunology
  • Microbial Pathogenesis

Background:

  • Eukaryotic protein regulation involves ubiquitination, a key process in immunity.
  • Pathogens exploit host ubiquitination to evade immune responses and manipulate cellular functions.
  • Prokaryotic pathogens lack intrinsic ubiquitination but can acquire related functions.

Purpose of the Study:

  • To explore how bacterial pathogens acquire and utilize ubiquitination machinery.
  • To understand the mechanisms of immune evasion and host process reprogramming by pathogens.
  • To investigate the role of gene transfer and evolution in bacterial ubiquitination mimicry.

Main Methods:

  • Analysis of effector molecules delivered by pathogens into host cells.
  • Investigation of horizontal and lateral gene transfer mechanisms in bacteria.
  • Study of convergent evolution shaping bacterial proteins for ubiquitination functions.

Main Results:

  • Pathogens deliver effector molecules mimicking host ubiquitination components.
  • Horizontal gene transfer enables bacteria to acquire host ubiquitination enzymes.
  • Lateral gene transfer facilitates the spread of ubiquitination functions within microbial communities.
  • Convergent evolution results in bacterial proteins with novel ubiquitination capabilities.

Conclusions:

  • Bacterial pathogens effectively mimic host ubiquitination systems for immune suppression.
  • Gene flow, including horizontal and lateral gene transfer, is crucial for bacterial acquisition of ubiquitination functions.
  • Convergent evolution also contributes to the development of bacterial ubiquitination mimicry, enhancing pathogen survival and spread.