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

8.5K
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....
8.5K
Phosphorylation01:02

Phosphorylation

53.4K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
53.4K
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

1.3K
The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
1.3K
Amyloid Fibrils03:03

Amyloid Fibrils

11.5K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
11.5K
The Proteasome01:13

The Proteasome

1.5K
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...
1.5K
The Proteasome02:18

The Proteasome

9.9K
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...
9.9K

You might also read

Related Articles

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

Sort by
Same author

Hyperdiploidy impairs fetal hematopoietic progenitor fitness and differentiation enabling persistence of rare preleukemic aneuploid clones.

Cell reports·2026
Same author

CRISPR-engineered human GATA2 deficiency model uncovers mitotic dysfunction and premature aging in HSPCs, impairing hematopoietic fitness.

Leukemia·2025
Same author

Backtracking NOM1::ETV6 fusion to neonatal pathogenesis of t(7;12) (q36;p13) infant AML.

Leukemia·2024
Same author

Integrative single-cell expression and functional studies unravels a sensitization to cytarabine-based chemotherapy through HIF pathway inhibition in AML leukemia stem cells.

HemaSphere·2024
Same author

Androgen deprivation induces double-null prostate cancer via aberrant nuclear export and ribosomal biogenesis through HGF and Wnt activation.

Nature communications·2024
Same author

Editorial: Chromosome segregation and aneuploidy in cancer.

Frontiers in cell and developmental biology·2024

Related Experiment Video

Updated: Dec 26, 2025

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
08:33

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

7.8K

SUMOylation in development and neurodegeneration.

Tak-Yu Yau1, Oscar Molina1, Albert J Courey2

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095-1569, USA.

Development (Cambridge, England)
|March 20, 2020
PubMed
Summary

Small ubiquitin-related modifier (SUMO)ylation is a crucial protein modification in eukaryotes, impacting development, signal transduction, and gene transcription. This process is also implicated in neurodegenerative diseases and may promote neuronal stem cell survival.

Keywords:
EpigeneticsNeurodegenerative disorderPost-translational protein modificationSUMOSignal transductionUbiquitin-like protein

More Related Videos

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

9.6K
Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells

Published on: October 10, 2017

9.3K

Related Experiment Videos

Last Updated: Dec 26, 2025

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
08:33

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

7.8K
In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

9.6K
Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells

Published on: October 10, 2017

9.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proteins are modified by small ubiquitin-related modifier (SUMO)ylation, a process essential for eukaryotic development.
  • SUMOylation alters protein function in specific spatial and temporal contexts.

Purpose of the Study:

  • To explain the mechanism of SUMOylation.
  • To summarize SUMOylation's regulatory roles in signal transduction and epigenetic control of transcription.
  • To evaluate SUMOylation's involvement in neurodegenerative disorders and neuronal stem cell functions.

Main Methods:

  • Literature review and synthesis of existing research on SUMOylation.
  • Analysis of SUMOylation's impact on various biological pathways.
  • Evaluation of SUMOylation's role in disease etiology and potential therapeutic applications.

Main Results:

  • SUMOylation regulates signal transduction pathways.
  • SUMOylation plays significant roles in the epigenetic control of transcription.
  • SUMOylation is implicated in Parkinson's disease and cerebral ischemia.
  • SUMOylation may enhance neuronal stem cell survival and neurogenesis.

Conclusions:

  • SUMOylation is a fundamental post-translational modification with broad biological significance.
  • Understanding SUMOylation is critical for comprehending development, gene regulation, and neurological disorders.
  • Targeting SUMOylation pathways may offer therapeutic strategies for neurodegenerative diseases and stem cell applications.