Related Experiment Video
Updated: Jan 27, 2026

08:51
Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification
Published on: November 19, 2018
10.2K
Mitotic functions of poly(ADP-ribose) polymerases
1Department of Biochemistry, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter (VBC), Dr. Bohr-gasse 9, 1030 Vienna, Austria.
Biochemical Pharmacology
|March 27, 2019
Summary
Poly(ADP-ribose) polymerases (PARPs) and PARG are crucial for mitosis. Inhibiting PARP1/2 causes replication stress and mitotic defects, making cancer cells vulnerable to combination therapies targeting cell division.
Area of Science:
- Cell Biology
- Molecular Biology
- Cancer Biology
Background:
- Mitosis requires precise regulation of DNA segregation.
- Poly(ADP-ribose) polymerases (PARPs) and PARG are key regulators of mitotic processes.
- PARP dysfunction leads to mitotic abnormalities.
Purpose of the Study:
- To review the mitotic roles of PARPs and PARG.
- To detail mitotic defects caused by PARP depletion or inhibition.
- To explore the therapeutic potential of targeting mitosis and replication stress.
Main Methods:
- Literature review of PARP and PARG functions in mitosis.
- Analysis of mitotic phenotypes resulting from PARP inhibition.
- Examination of therapeutic strategies combining PARP inhibition with other treatments.
Main Results:
- PARP1/2 inhibition induces replication stress and DNA damage, leading to mitotic defects.
- These defects include centrosome amplification, spindle abnormalities, and chromosomal aberrations.
- Cancer cells with high replication stress are sensitive to combined therapies targeting PARP and DNA repair.
Conclusions:
- PARPs and PARG are essential for accurate mitosis.
- PARP inhibition creates vulnerabilities in cancer cells by inducing replication stress and mitotic errors.
- Targeting mitotic functions and replication stress presents promising therapeutic avenues for cancer treatment.
Related Concept Videos
Bacterial RNA Polymerase
32.6K
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
32.6K
Bacterial RNA Polymerase
11.7K
11.7K
The ADP/ATP Carrier Protein
4.2K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
4.2K
The Mitotic Spindle
7.9K
The mitotic spindle—or spindle apparatus—is a eukaryotic, cytoskeletal structure made up of long protein fibers called microtubules. Formed during cell division, the spindle separates sister chromatids and moves them to opposite ends of a parental cell, where the now individual chromosomes are distributed to two daughter cell nuclei.
The bipolar configuration of the mitotic spindle facilitates chromosomal segregation, preparing the cell for division. One mechanism that ensures...
The bipolar configuration of the mitotic spindle facilitates chromosomal segregation, preparing the cell for division. One mechanism that ensures...
7.9K
Translesion DNA Polymerases
11.1K
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
11.1K
Eukaryotic RNA Polymerases
26.8K
RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
All three eukaryotic RNAPs require specific transcription factors, of which the...
26.8K

