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

Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

10.5K
The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...
10.5K
Regulated Protein Degradation02:58

Regulated Protein Degradation

7.1K
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...
7.1K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

7.5K
Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
7.5K
mRNA Stability and Gene Expression02:51

mRNA Stability and Gene Expression

5.5K
The structure and stability of mRNA molecules regulates gene expression, as mRNAs are a key step in the pathway from gene to protein. In eukaryotes, the half-life of mRNA varies from a few minutes up to several days. mRNA stability is essential in growth and development. The absence of the proteins regulating its stability, such as tristetraprolin in mice, can cause systemic issues, including bone marrow overgrowth, inflammation, and autoimmunity.
Cis-acting Elements involved in mRNA stability
5.5K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.4K
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...
2.4K
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

2.8K
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...
2.8K

You might also read

Related Articles

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

Sort by
Same author

Tislelizumab-induced myositis antibody-negative myasthenia gravis in patients with urothelial carcinoma: a case report.

Frontiers in immunology·2026
Same author

An AI-powered diagnostic system for grading and invasion of non-muscle-invasive bladder cancer via TURBT specimens: A multicenter study.

iScience·2026
Same author

Epigallocatechin gallate targets the hexokinase 2-voltage-dependent anion channel 1 axis in myofibroblasts to attenuate pulmonary fibrosis.

Phytomedicine : international journal of phytotherapy and phytopharmacology·2026
Same author

Single-Cell Transcriptomic Landscape of Smoking-Related Periodontitis.

Oral diseases·2026
Same author

STRAP promotes hepatocellular carcinoma progression through activation of an STRAP/Wnt-β-catenin/STRAP positive feedback loop.

iScience·2026
Same author

Spectral CT-based intratumoral and peritumoral radiomics for predicting invasiveness of ground-glass nodules in lung adenocarcinoma.

La Radiologia medica·2026

Related Experiment Video

Updated: Jun 3, 2025

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

6.6K

Cul3 substrate adaptor SPOP targets Nup153 for degradation.

Joseph Y Ong1, Mai Abdusamad1, Ivan Ramirez1

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095.

Molecular Biology of the Cell
|January 9, 2025
PubMed
Summary

The study identifies Nuclear Pore Protein 153 (Nup153) as a novel substrate of Speckle-type POZ protein (SPOP). SPOP regulates Nup153 levels, impacting cell proliferation and homeostasis.

More Related Videos

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast
07:31

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast

Published on: June 30, 2022

2.4K
Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
09:05

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

28.9K

Related Experiment Videos

Last Updated: Jun 3, 2025

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

6.6K
ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast
07:31

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast

Published on: June 30, 2022

2.4K
Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
09:05

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

28.9K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Speckle-type POZ protein (SPOP) is a crucial E3 ubiquitin ligase adaptor regulating protein degradation.
  • Dysregulation of SPOP is implicated in cancer progression by affecting cell growth and proliferation.
  • Understanding SPOP substrates is key to deciphering its role in cellular homeostasis.

Purpose of the Study:

  • To identify novel substrates of SPOP.
  • To investigate the functional relationship between SPOP and its newly identified substrate, Nup153.
  • To elucidate the impact of SPOP-Nup153 interaction on cellular processes.

Main Methods:

  • Co-immunoprecipitation to confirm SPOP-Nup153 binding.
  • Immunofluorescence microscopy to assess subcellular localization.
  • RNA interference (RNAi) to deplete SPOP levels.
  • Western blotting to analyze protein stability.

Main Results:

  • Nuclear Pore Protein 153 (Nup153) was identified as a novel SPOP substrate.
  • SPOP and Nup153 interact and colocalize at the nuclear envelope.
  • SPOP mediates Nup153 ubiquitylation and degradation; SPOP depletion stabilizes Nup153.
  • Loss of SPOP enhances nuclear envelope localization of Mad1, a protein tethered by Nup153.

Conclusions:

  • SPOP directly regulates Nup153 protein levels.
  • This regulation impacts nuclear pore complex function and spindle assembly checkpoint.
  • Findings expand the understanding of SPOP's role in protein homeostasis and cell proliferation control.