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

Regulated Protein Degradation02:58

Regulated Protein Degradation

6.5K
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...
6.5K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
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...
2.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
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....
8.2K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

1.3K
1.3K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.5K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.5K
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

2.0K
Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
2.0K

You might also read

Related Articles

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

Sort by
Same author

KREPA6 functions in RNA editing catalytic complex structural organization and gRNA utilization in Trypanosoma brucei.

Nucleic acids research·2026
Same author

Discovery and Characterization of Divarasib (GDC-6036), a Potent Covalent Inhibitor of KRAS G12C.

Journal of medicinal chemistry·2026
Same author

VIF-Ig: a novel fc framework for ADCC by incorporation of VHH unit.

Protein engineering, design & selection : PEDS·2026
Same author

Development of a bispecific antibody that inhibits EGFR and B7H3 in NSCLC.

Biomarker research·2025
Same author

Differential regulation of the eicosanoid biosynthesis pathway in response to Enterocytozoon hepatopenaei infection in Litopenaeus vannamei.

PloS one·2025
Same author

Boosting softwood hemicellulose hydrolysis: Enzymes from a new fungi Penicillium rotoruae remarkably improve CTec-2 hydrolysis efficiency and reduce sugar production costs.

Bioresource technology·2025
Same journal

Shikonin sensitizes A549 cells to TRAIL-induced apoptosis through the JNK, STAT3 and AKT pathways.

BMC cell biology·2018
Same journal

Mitotic activity patterns and cytoskeletal changes throughout the progression of diapause developmental program in Daphnia.

BMC cell biology·2018
Same journal

Post-treatment de-phosphorylation of p53 correlates with dasatinib responsiveness in malignant melanoma.

BMC cell biology·2018
Same journal

Comparative evaluation of mesenchymal stromal cells from umbilical cord and amniotic membrane in xeno-free conditions.

BMC cell biology·2018
Same journal

The STRIPAK complex components FAM40A and FAM40B regulate endothelial cell contractility via ROCKs.

BMC cell biology·2018
Same journal

Kif17 phosphorylation regulates photoreceptor outer segment turnover.

BMC cell biology·2018
See all related articles

Related Experiment Video

Updated: Apr 27, 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

7.7K

Novel Cul3 binding proteins function to remodel E3 ligase complexes.

Wananit Wimuttisuk, Mark West, Brittney Davidge

  • 1Department of Biology, Portland State University, Portland, Oregon, USA. jsinger@pdx.edu.

BMC Cell Biology
|July 12, 2014
PubMed
Summary
This summary is machine-generated.

Researchers identified novel Cul3-binding proteins (CLWs) that regulate ubiquitin ligase complexes. These CLWs alter BTB protein binding, leading to BTB protein degradation, offering a new regulatory mechanism for the Cullin3-based BCR complex.

More Related Videos

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
05:35

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

Published on: March 3, 2016

15.0K
In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

5.3K

Related Experiment Videos

Last Updated: Apr 27, 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

7.7K
Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
05:35

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

Published on: March 3, 2016

15.0K
In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

5.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Cullin proteins form multi-subunit ubiquitin ligase complexes for protein ubiquitination.
  • Cullin3 (Cul3) assembles the BTB-Cul3-Rbx1 (BCR) ubiquitin ligase complex.
  • BTB domain-containing proteins in the BCR complex are thought to act as both substrate adaptors and recognition proteins.

Purpose of the Study:

  • To identify novel Cul3-binding proteins.
  • To elucidate the function of Cul3-binding proteins within the BCR ubiquitin ligase complex.

Main Methods:

  • Tandem affinity purification and Liquid Chromatography-Tandem Mass Spectrometry (LC/MS-MS) were employed to analyze the BCR complex.
  • Bioinformatic analysis using SEQUEST and CDART programs for protein identification and domain prediction.
  • Biochemical assays to determine binding interactions and substrate identification through modified lysine residue analysis.

Main Results:

  • A novel group of Cul3-binding proteins containing leucine-rich repeats (LRR) or WD40 domains (CLWs) were identified.
  • Biochemical analysis demonstrated that LRR-containing CLWs bind to both Cul3 and BTB domain proteins.
  • CLWs were found to modify the binding of BTB proteins, potentially marking them for degradation, and were not identified as substrates themselves.

Conclusions:

  • The study successfully identified CLWs as a new class of Cul3-binding proteins.
  • Certain CLWs play a regulatory role by altering the interaction of BTB proteins within the BCR complex, leading to BTB protein degradation.
  • CLWs represent a unique mechanism for regulating the activity of the Cul3-based ubiquitin ligase complex.