Suv39H1: A Key Regulator of Cell Proliferation and Cancer (G6839)

Target Name: SUV39H1

NCBI ID: G6839

Suv39H1: A Key Regulator of Cell Proliferation and Cancer

SUV39H1, also known as suppressor of variegation 3-9 homolog 1, is a protein that is expressed in various tissues throughout the body. It is a key regulator of cell proliferation and has been identified as a potential drug target for various diseases, including cancer.

The SUV39H1 protein is named after its discoverer, Dr. Yasmina Boudjemaa, a renowned oncologist at the University of Montreal. Dr. Boudjemaa's research has focused on the role of SUV39H1 in cancer progression and the development of new treatments.

Suv39h1 is a 21-kDa protein that is expressed in a variety of tissues, including muscle, heart, brain, and various cancers. It is a key regulator of cell proliferation and has been shown to play a role in the development and progression of various diseases.

One of the most significant functions of SUV39H1 is its ability to suppress the formation of new blood vessels in tumors. This is a critical step in the development of cancer, as blood vessels provide the necessary oxygen and nutrients to fuel tumor growth. By inhibiting the formation of new blood vessels, SUV39H1 may be able to limit the growth of tumors and reduce their ability to spread.

Suv39H1 has also been shown to play a role in the regulation of cell apoptosis, or cell death. In cancer cells, apoptosis is a natural response to the development of a cancerous tumor. However, in some cancer cells, apoptosis may be exploited by the tumor to continue growing and dividing. By promoting apoptosis in cancer cells, SUV39H1 may be able to contribute to the development of new treatments for cancer.

Another function of SUV39H1 is its role in the regulation of cell signaling pathways. Specifically, it has been shown to play a negative role in the PI3K/Akt signaling pathway. This pathway is involved in the regulation of cell proliferation and survival, and is a key target for many drugs used in the treatment of cancer. By inhibiting the activity of SUV39H1, researchers may be able to develop new treatments for cancer that are less invasive and more effective.

Suv39H1 has also been shown to play a role in the regulation of stem cell proliferation. Stem cells are a vital source of cancer cells, and the regulation of stem cell proliferation is critical for the development and maintenance of cancer. a negative role in the regulation of stem cell proliferation, which may be important for the development of new treatments for cancer.

In conclusion, SUV39H1 is a protein that has been shown to play a critical role in the development and progression of various diseases. Its functions as a regulator of cell proliferation and apoptosis, as well as its role in the regulation of signaling pathways and stem cell proliferation make it an attractive target for research into new treatments for cancer. Further research is needed to fully understand the role of SUV39H1 in cancer and to develop new treatments based on its properties.

Protein Name: SUV39H1 Histone Lysine Methyltransferase

Functions: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation

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