PARP9: The Parkin Gene's Unlocked Potential (G83666)

Target Name: PARP9

NCBI ID: G83666

PARP9

PARP9: The Parkin Gene's Unlocked Potential

Parp9 is a gene located on chromosome 1p36.2, which is responsible for encoding the protein Parkin. Parkin is a non-histone nuclear protein that plays a crucial role in the regulation of DNA replication, repair, and toss, which are essential processes for the maintenance of genomic stability.parkin's dysfunction has been implicated in various diseases, including cancer, neurodegenerative diseases, and developmental disorders. Although PARP9 has been studied extensively, its functions and potential drug targets remain poorly understood. In this article, we will explore the PARP9 gene, its functions, potential drug targets, and the research being conducted to unlock its potential.

FUNCTIONS OF PARP9

Parkin is a 21-kDa protein that is expressed in various tissues and cells throughout the body. It is composed of a unique nucleotide-binding domain, a transmembrane region, and a cytoplasmic tail. The nucleotide-binding domain is the region where PARP9 interacts with DNA, while the transmembrane region is responsible for the protein's localization to the membrane, and the cytoplasmic tail is involved in the protein's stability and interactions with other cellular components.

One of the most significant functions of PARP9 is its role in DNA replication. During DNA replication, PARP9 is involved in the formation of a complex with the DNA template, where it interacts with the template's double helix. This interaction is critical for the proper execution of the replication process, as double-strand break repair (DSBR) is a critical component of DNA replication.

In addition to its role in DNA replication, PARP9 is also involved in the regulation of DNA repair. When DNA double-strand breaks occur, PARP9 helps to ensure that the repair process is executed correctly. It does this by promoting the formation of a complex with the DNA template at the break site, which allows the template to be effectively repaired by the repair machinery.

Another function of PARP9 is its role in the regulation of cell division. PARP9 is involved in the determination of the interphase of cell division, which is the stage of the cell cycle where the nuclear envelope is laid down and the chromosomes become visible. During interphase, PARP9 interacts with the centromere, which is the region of the chromosome that is responsible for proper attachment of the nuclear envelope during mitosis.

POTENTIAL DRUG SOURCES

The PARP9 gene has been a target of intense research in recent years, with a focus on its potential as a drug target. Several studies have suggested that PARP9 may be a useful target for cancer therapy, particularly in the context of neurodegenerative diseases.

One of the reasons for the interest in PARP9 as a cancer target is its role in cell division. PARP9 is involved in the regulation of cell division, and it has been shown to play a role in the development of cancer. For example, studies have shown that PARP9 is overexpressed in various types of cancer, including breast, ovarian, and colorectal cancer. This suggests that targeting PARP9 may be an effective way to treat cancer.

Another potential drug target for PARP9 is its role in neurodegenerative diseases.PARP9 has been shown to be involved in the development and progression of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. Studies have shown that PARP9 is overexpressed in the brains of individuals with these conditions, and that targeting PARP9 may be an effective way to treat these

Protein Name: Poly(ADP-ribose) Polymerase Family Member 9

Functions: ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses (PubMed:16809771, PubMed:23230272, PubMed:26479788, PubMed:27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (PubMed:28525742). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones (PubMed:28525742). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (PubMed:23230272). Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272, PubMed:28525742). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ); the complex function is negatively modulated by PARP9 activity (PubMed:28525742). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (By similarity). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation (PubMed:27796300). Also suppresses PARP14-mediated STAT6 ADP-ribosylation (PubMed:27796300)

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•   the target screening and validation;
•   expression level;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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