Related Experiment Video
Updated: Mar 1, 2026

11:36
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
11.6K
Ubiquitination and SUMOylation in Telomere Maintenance and Dysfunction.
Zeliha Yalçin1, Carolin Selenz1, Jacqueline J L Jacobs1
1Department of Molecular Oncology, Netherlands Cancer InstituteAmsterdam, Netherlands.
Frontiers in Genetics
|June 8, 2017
Summary
Telomeres protect chromosome ends, but shorten with cell division, leading to aging and cancer. Recent research highlights how ubiquitination and SUMOylation are crucial for telomere maintenance and function.
Area of Science:
- Molecular Biology
- Genetics
- Cell Biology
Background:
- Telomeres are protective structures at chromosome ends.
- Telomere shortening limits cell proliferation and impacts aging and cancer.
- Post-translational modifications are increasingly recognized in telomere biology.
Purpose of the Study:
- To review recent findings on post-translational modifications at telomeres.
- To highlight the roles of ubiquitination and SUMOylation in telomere maintenance and dysfunction.
Main Methods:
- Literature review of recent studies.
- Focus on ubiquitination and SUMOylation pathways at telomeres.
Main Results:
- Ubiquitination and SUMOylation play essential roles in telomere maintenance.
- These modifications are involved in regulating telomere replication and preventing telomere dysfunction.
- Dysfunctional telomeres trigger DNA damage responses, impacting cellular fate.
Conclusions:
- Ubiquitination and SUMOylation are critical for genome integrity via telomere regulation.
- Understanding these modifications offers insights into aging and tumorigenesis.
- Further research into telomere post-translational modifications is warranted.
Related Concept Videos
Telomeres and Telomerase
27.7K
In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded...
27.7K
Telomeres and Telomerase
7.6K
7.6K
Replication in Eukaryotes
18.1K
In eukaryotic cells, DNA replication is highly conserved and tightly regulated. Multiple linear chromosomes must be duplicated with high fidelity before cell division, so there are many proteins that fulfill specialized roles in the replication process. Replication occurs in three phases: initiation, elongation, and termination, and ends with two complete sets of chromosomes in the nucleus.
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...
18.1K
Replication in Eukaryotes
206.4K
Overview
206.4K
Replicative Cell Senescence
4.5K
Replicative cell senescence is a property of cells that allows them to divide a finite number of times throughout the organism's lifespan while preventing excessive proliferation. Replicative senescence is associated with the gradual loss of the telomere — short, repetitive DNA sequences found at the end of the chromosomes. Telomeres are bound by a group of proteins to form a protective cap on the ends of chromosomes. Embryonic stem cells express telomerase — an enzyme that adds...
4.5K
Covalently Linked Protein Regulators
9.8K
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....
These groups modify specific amino acids in a protein....
9.8K

