Related Experiment Video
Updated: Jul 26, 2025
05:35
Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
Published on: March 3, 2016
15.3K
The E3 ligase Poe promotes Pericentrin degradation.
Brian J Galletta1, Ramya Varadarajan1, Carey J Fagerstrom1
1Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, and.
Molecular Biology of the Cell
|June 21, 2023
Summary
Protein levels of Pericentrin-like protein (PLP) are tightly controlled in male germ cells through ubiquitin-mediated degradation. This regulation is crucial for proper centriole function and positioning.
Area of Science:
- Cell Biology
- Molecular Biology
- Developmental Biology
Background:
- Centrosomes are vital for cellular functions, requiring precise protein level regulation.
- Pericentrin (PCNT) and Pericentrin-like protein (PLP) are key centrosomal proteins.
- Dysregulation of PCNT is linked to cancer, mental disorders, and ciliopathies.
Purpose of the Study:
- To investigate the mechanisms regulating Pericentrin-like protein (PLP) levels during male germ cell development.
- To identify proteins involved in PLP degradation.
- To understand the functional consequences of PLP dysregulation.
Main Methods:
- Ubiquitin-mediated degradation assays.
- Identification of E3 ligases interacting with PLP.
- Analysis of PLP localization and centriole function in genetically modified cells.
Main Results:
- PLP undergoes ubiquitin-mediated degradation in spermatocytes.
- The E3 ligase Poe (UBR4) binds to PLP and promotes its degradation.
- Stabilization of PLP leads to its accumulation, mispositioning on centrioles, and defects in centriole docking.
Conclusions:
- Poe-mediated degradation is essential for controlling PLP levels during spermatogenesis.
- Proper PLP regulation is critical for correct centriole positioning and function.
- Understanding PLP regulation provides insights into centrosome-related disorders.
More Related Videos
Related Concept Videos
02:58Regulated Protein Degradation
7.4K
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...
7.4K
01:32Export of Misfolded Proteins out of the ER
3.7K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.7K
00:50Anaphase Promoting Complex
2.9K
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...
2.9K
01:22Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal
2.3K
Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
2.3K
01:45Tail-anchoring of Proteins in the ER Membrane
3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
01:37The Unfolded Protein Response
4.8K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
4.8K