Related Experiment Video
Updated: May 2, 2026
11:36
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
10.6K
Regulation of stem cell function by protein ubiquitylation
Alexandros Strikoudis1, Maria Guillamot, Iannis Aifantis
1Howard Hughes Medical Institute New York University School of Medicine, New York, NY, USA.
EMBO Reports
|March 22, 2014
Summary
Ubiquitylation, a key protein modification, regulates stem cell fate by controlling cell stability and function. Dysregulation of these processes can lead to tumor-initiating cells.
Area of Science:
- Cell Biology
- Molecular Biology
- Stem Cell Biology
Background:
- Tissue homeostasis relies on stem cells producing functional progeny.
- Stem cell behavior is regulated by environmental signals, transcriptional networks, and chromatin factors.
- Post-translational modifications, particularly ubiquitylation, are increasingly recognized as critical regulators.
Purpose of the Study:
- To review the role of ubiquitylation in embryonic and adult multipotent stem cells.
- To analyze mechanisms controlling stem cell quiescence, self-renewal, and differentiation.
- To discuss how aberrant ubiquitin-mediated protein degradation contributes to tumor-initiating cells.
Main Methods:
- Literature review of ubiquitylation's role in stem cell systems.
- Analysis of molecular mechanisms governing stem cell fate decisions.
- Examination of links between protein degradation pathways and cancer stem cells.
Main Results:
- Ubiquitylation impacts stem cell stability and function, influencing key regulatory factors.
- Specific ubiquitylation pathways dictate the balance between stem cell quiescence, self-renewal, and differentiation.
- Disrupted ubiquitin-mediated protein degradation is implicated in the development of tumor-initiating cells.
Conclusions:
- Ubiquitylation is a central post-translational modification governing stem cell fate.
- Understanding ubiquitylation mechanisms is crucial for maintaining tissue homeostasis and preventing diseases like cancer.
- Targeting ubiquitin pathways may offer therapeutic strategies for stem cell-related disorders and cancer.
Related Concept Videos
02:58Regulated Protein Degradation
6.6K
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...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
6.6K
02:58Regulated Protein Degradation
2.5K
2.5K
02:04Covalently 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....
These groups modify specific amino acids in a protein....
8.2K
01:23Regulation of Expression at Multiple Steps
1.4K
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...
1.4K
01:45Regulation 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
01:13The Proteasome
1.6K
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...
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...
1.6K