Related Experiment Video
Updated: Jan 18, 2026
08:16
Author Spotlight: Exploring the Frontier of mRNA Research with Poly A Tail Analysis Techniques
Published on: January 12, 2024
1.4K
Disordered Protein Tail Is Wagging Poly(ADP-ribosyl)ation.
Guillaume Bordet1, Yaroslava Karpova1, Saraynia Espeseth1
1Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 North Columbia Road, Stop 9061, Grand Forks, ND 58202, USA.
International Journal of Molecular Sciences
|September 13, 2025
Summary
The disordered tail of Poly(ADP-ribose) glycohydrolase (PARG) controls its localization and activity. This regulatory hub ensures proper function by interacting with nuclear factors and chromatin.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Intrinsically disordered regions (IDRs) are prevalent in proteins, lacking conserved structure but maintaining function.
- The disordered tail of Poly(ADP-ribose) glycohydrolase (PARG) was previously uncharacterized.
Purpose of the Study:
- To investigate the function of the disordered tail region of PARG.
- To understand how this region controls PARG's localization and enzymatic activity.
Main Methods:
- Protein deletion analysis
- Mass spectrometry
- Subcellular localization studies
Main Results:
- Deletion of the PARG disordered tail caused mislocalization to the cytoplasm and nucleolus.
- The disordered tail deletion impaired chromatin association and reduced enzymatic activity.
- Mass spectrometry identified interactions with nuclear transport and chromatin-associated factors.
Conclusions:
- The disordered tail of PARG is a critical regulatory hub.
- This region integrates multiple controls for PARG's subcellular localization and chromatin function.
- The disordered tail supports conserved regulatory functions across species despite structural divergence.
Related Concept Videos
01:45Tail-anchoring of Proteins in the ER Membrane
3.7K
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...
3.7K
01:32Export of Misfolded Proteins out of the ER
5.0K
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...
5.0K
01:37The Unfolded Protein Response
6.3K
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...
6.3K
01:29Protein Folding Quality Check in the RER
5.0K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.0K
02:04Covalently Linked Protein Regulators
8.7K
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....
8.7K
02:11Proteins: From Genes to Degradation
14.1K
Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick. Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
Transcription is the synthesis of RNA...
14.1K