The Nuclear Receptor Binding SET Domain Protein 2: A Promising Drug Target and Biomarker

Target Name: NSD2

NCBI ID: G7468

NSD2

The Nuclear Receptor Binding SET Domain Protein 2: A Promising Drug Target and Biomarker

The Nuclear Receptor Binding SET Domain Protein 2 (NSD2) is a key transcription factor that regulates various cellular processes. It plays a vital role in the development, maintenance, and progression of tissues, including cancer. The NSD2 gene has four splice variants, which result in different isoforms with distinct nuclear localization patterns. Transcript variant 10 (NSD2-T10) is a widely expressed isoform, and it has been implicated in various physiological processes. The purpose of this article is to discuss the potential implications of NSD2-T10 as a drug target and biomarker.

NSD2-T10: A Potential Drug Target

The NSD2 gene is known to play a critical role in the development and maintenance of tissues, including the nervous system and endocrine system. It contains a unique SET domain that is involved in nuclear receptor binding. This domain is known to interact with various nuclear receptors, which are responsible for transmitting signals from the cytoplasm to the nucleus. The NSD2-T10 gene has been implicated in the regulation of various cellular processes, including cell growth, differentiation, and survival.

Recent studies have suggested that NSD2-T10 can be a potential drug target in various diseases, including cancer. Several studies have shown that inhibiting the activity of NSD2-T10 can lead to the inhibition of various cellular processes that are associated with disease progression. For example, in cancer cells, the NSD2-T10 gene has been shown to promote the growth and survival of these cells. By inhibiting the activity of NSD2-T10, researchers have found that they can significantly reduce the growth and survival of cancer cells.

NSD2-T10 also plays a role in the regulation of cellular signaling pathways. The NSD2-T10 gene has been shown to be involved in the regulation of various signaling pathways, including the TGF-β pathway. This pathway is involved in the regulation of cell growth, differentiation, and survival, and is a key factor in the development and maintenance of tissues. By targeting the NSD2-T10 gene, researchers have found that they can disrupt various cellular processes that are associated with disease progression.

NSD2-T10 as a Biomarker

In addition to its potential as a drug target, NSD2-T10 has also been shown to be a potential biomarker for various diseases. The NSD2-T10 gene has been shown to be involved in the regulation of various cellular processes, including cell growth, differentiation, and survival. This suggests that it may be a useful biomarker for various diseases.

One of the key advantages of using NSD2-T10 as a biomarker is its stability. The NSD2-T10 gene has been shown to be highly stable, which makes it a potential marker for long-term disease outcomes. This stability is also a key factor in the reliability of gene expression assays, which are often used to measure the expression of NSD2-T10 in patient samples.

Another advantage of NSD2-T10 as a biomarker is its potential to be used in multiplexed assays. Multiplexed assays are used to measure the expression of multiple genes in a single assay, which can increase the sensitivity and specificity of disease diagnosis. By using NSD2-T10 as a biomarker in multiplexed assays, researchers have found that they can detect changes in gene expression associated with disease progression more accurately than with single-gene assays.

Conclusion

In conclusion, the Nuclear Receptor Binding SET Domain Protein 2 (NSD2-T10) is a potential drug target and biomarker for various diseases. Its stability and potential to be used in multiplexed assays make it an attractive candidate for use in drug development and disease diagnosis. Further research is needed to fully understand the role of NSD2-T10 in

Protein Name: Nuclear Receptor Binding SET Domain Protein 2

Functions: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:27571355, PubMed:22099308, PubMed:19808676, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity). By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617). In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation (By similarity). During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes (By similarity). Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation (PubMed:29728617). During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation (By similarity). During B-cell development, required for the generation of the B1 lineage (By similarity). During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response (By similarity). Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation (By similarity). By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA (By similarity)

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