Related Experiment Video
Updated: Sep 8, 2025
10:06
Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells
Published on: April 26, 2017
9.0K
PLAA/UFD-3 regulates P-bodies through its intrinsic disordered domain.
Alakananda Das1, Yanping Qiu1, Trevor J Wolf1
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Summary
Phospholipase A2 activating protein (PLAA) regulates proteome homeostasis through distinct pathways. UFD-3, a PLAA ortholog, interacts with mRNA decapping complex proteins in P-bodies, separate from its role in protein degradation.
Area of Science:
- Cell Biology
- Molecular Biology
- Proteomics
Background:
- Proteome homeostasis is vital for eukaryotic survival and adaptation.
- Phospholipase A2 activating protein (PLAA) is implicated in ubiquitin-dependent protein degradation.
- The precise molecular targets and interaction network of PLAA are not fully understood.
Purpose of the Study:
- To investigate the neuronal interactors of the C. elegans PLAA ortholog UFD-3.
- To determine UFD-3's effect on ubiquitinated proteins and global protein expression.
- To elucidate the distinct roles of UFD-3 in protein degradation and mRNA regulation.
Main Methods:
- Proteome-scale approaches in Caenorhabditis elegans.
- Biochemical analysis in vitro.
- Fluorescence imaging in C. elegans.
Main Results:
- UFD-3 directly interacts with the mRNA decapping complex regulatory subunit DCAP-1.
- UFD-3's intrinsic disordered region (IDR) is crucial for recruiting DCAP-1 to P-bodies.
- Loss of the IDR does not impair UFD-3's function in the ubiquitin-dependent protein degradation pathway.
Conclusions:
- UFD-3 plays a role in cytoplasmic mRNA processing bodies (P-bodies).
- UFD-3's function in P-bodies is distinct from its role in ubiquitin-dependent protein degradation.
- PLAA/UFD-3 regulates proteome homeostasis via both protein turnover and mRNA regulation pathways.
Related Concept Videos
02:18Intrinsically Disordered Proteins
18.1K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.1K
02:04Covalently Linked Protein Regulators
7.1K
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....
7.1K
01:37The Unfolded Protein Response
5.1K
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...
5.1K
02:58Regulated Protein Degradation
7.6K
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...
7.6K
01:31Regulation of the Unfolded Protein Response
2.6K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.6K
01:38Intralumenal Vesicles and Multivesicular Bodies
3.7K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
3.7K