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

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
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....
9.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

2.1K
2.1K
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

3.5K
The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
3.5K
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

6.2K
The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
6.2K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
2.2K

You might also read

Related Articles

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

Sort by
Same author

Cryo-EM structures of higher order Gephyrin oligomers reveal principles of inhibitory postsynaptic scaffold organization.

Nature communications·2026
Same author

A structural code for assembly specificity in GID/CTLH-type E3 ligases.

eLife·2026
Same author

Aggregation-dependent epitope sequence and modification fingerprints of anti-Aβ antibodies.

eLife·2026
Same author

Microbial dl-Peptidases Enable Predator Defense and Facilitate Structure Elucidation of Complex Natural Products.

Journal of the American Chemical Society·2026
Same author

Inhibitors of GapN-dependent NADPH supply as potential lead compounds for novel therapeutics against <i>Streptococcus pyogenes</i>.

Virulence·2025
Same author

Crystal structure of the class V GTP-binding RNA aptamer bound to its ligand: GTP recognition by a topologically complex intermolecular G-quadruplex.

Nucleic acids research·2025

Related Experiment Video

Updated: Apr 4, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

8.8K

Control of p97 function by cofactor binding.

Alexander Buchberger1, Hermann Schindelin2, Petra Hänzelmann2

  • 1Department of Biochemistry, Biocenter, University of Würzburg, Am Hubland, 97074 Würzburg, Germany.

FEBS Letters
|September 1, 2015
PubMed
Summary

p97 ATPase, a key protein recycler, requires cofactors for substrate specificity. Understanding these interactions and disease-linked mutations is crucial for deciphering its cellular roles.

Keywords:
ATPases Associated with diverse cellular ActivitiesInclusion Body Myopathy with Paget́s disease of the bone and Fronto-temporal DementiaUBXD1UFD1-NPL4p47

More Related Videos

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

623
Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.3K

Related Experiment Videos

Last Updated: Apr 4, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

8.8K
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

623
Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.3K

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • p97 ATPase (also known as Cdc48, Ter94, and VCP) is a highly conserved protein essential for ubiquitylated protein turnover in eukaryotes.
  • p97 lacks intrinsic substrate specificity and relies on numerous regulatory cofactors to mediate its diverse cellular functions.
  • The intricate regulation of p97-cofactor interactions at temporal and spatial levels is a complex area of ongoing research.

Purpose of the Study:

  • To provide an overview of the structural framework governing p97 interactions with its cofactors.
  • To elucidate the emerging principles behind the assembly of p97-cofactor complexes.
  • To discuss the pathogenic consequences of disease-associated p97 mutations on cofactor binding.

Main Methods:

  • Structural analysis of p97-cofactor complexes.
  • Biochemical assays to study complex assembly.
  • Analysis of disease-associated mutations impacting cofactor interactions.

Main Results:

  • Detailed structural insights into the p97-cofactor interaction landscape.
  • Identification of key principles governing the dynamic assembly of functional p97 complexes.
  • Demonstration of how specific p97 mutations disrupt cofactor binding and cellular function.

Conclusions:

  • p97 cofactor interactions are critical for its diverse cellular roles and substrate specificity.
  • Understanding these interactions provides a framework for investigating p97-related cellular dysfunction.
  • Insights into disease-associated mutations highlight the importance of precise p97-cofactor regulation.