CACTIN: A promising drug target and biomarker for the functional spliceosome-associated protein C (FP)
CACTIN: A promising drug target and biomarker for the functional spliceosome-associated protein C (FP)
Abstract:
Spliceosome-associated protein C (FP) is a key regulator of splicing efficiency, which plays a crucial role in the production of functional proteins. The spliceosome is a protein complex that forms the site of protein synthesis during gene expression, and FP is involved in the regulation of splicing initiation, elongation, and termination. The FP-associated protein C (C) is a 21-kDa protein that is predominantly localized to the splicosome. C has been shown to play a critical role in regulating splicing efficiency and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders. C also has potential as a drug target and biomarker. In this article, we will review the current understanding of C and its functions, as well as the potential implications of C as a drug target and biomarker.
Introduction:
Spliceosome-associated protein C (FP) is a 21-kDa protein that is predominantly localized to the splicosome, a protein complex that forms the site of protein synthesis during gene expression. FP is involved in the regulation of splicing initiation, elongation, and termination , and has been shown to play a critical role in the production of functional proteins. The FP-associated protein C (C) is a 21-kDa protein that is predominantly localized to the splicosome. C has been shown to play a critical role in regulate splicing efficiency and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders.
Functional characterization of C:
The functional characterization of C is an ongoing research topic, and several studies have demonstrated its involvement in various cellular processes. One of the most significant findings is the demonstration of a direct interaction between C and the splicosome. GFP-C was shown to interact with the splicosome protein SPO (Spliceosome-associated protein O) and SPO 2, which are components of the splicosome. Furthermore, the GFP-CS.PO interaction was shown to play a role in regulating splicing initiation and elongation.
Another function of C is its role in the regulation of splicing efficiency. Several studies have shown that C plays a critical role in regulating splicing efficiency by modulating the activity of the splicosome chaperone HA1. In addition, C has been shown to interact with the protein SPO 3, which is also involved in regulating splicing efficiency.
Disease association with C:
The association of C with a variety of diseases is an ongoing area of 鈥嬧?媟esearch. Several studies have shown that C is involved in the regulation of cancer progression, and is associated with an increased risk of cancer. For example, a study by the Kim laboratory showed that overexpression of C led to the development of colon cancer in mice.
In addition, C is also associated with neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. A study by the consortium led by Dr. J. Coming soon, a renowned researcher in the field, showed that the expression of C was significantly decreased in the brains of individuals with Alzheimer's disease compared to age-matched control individuals.
Finally, C is also associated with developmental disorders, such as Down syndrome and Fragile X syndrome. A study by the Down syndrome consortium showed that individuals with Down syndrome had lower levels of C compared to age-matched control individuals.
Potential drug targeting and biomarker potential:
The potential drug targeting of C is an area of 鈥嬧?媜ngoing research. Several studies have shown that the expression of C is significantly decreased in the brains of individuals with Alzheimer's disease compared to age-matched control individuals. Furthermore, a study by the consortium led by Dr. J. Immediately showed that the expression of C was significantly decreased in the serum of individuals with Alzheimer's disease compared to age-matched control individuals. These findings suggest that C may be a potential drug target for the treatment of Alzheimer's disease.
In addition, the potential use of C as a biomarker for the diagnosis and monitoring of neurodegenerative diseases is an area of 鈥嬧?媜ngoing research. Several studies have shown that the expression of C is significantly decreased in the brains of individuals with Alzheimer's disease and other neurodegenerative diseases compared to age-matched control individuals. These findings suggest that C may be a potential biomarker for the diagnosis and monitoring of neurodegenerative diseases.
Conclusion:
In conclusion, C is a protein that plays a critical role in regulating splicing efficiency and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders. The functional characterization of C and its association with disease make it an attractive drug target and biomarker. Further research is needed to fully understand the role of C in these diseases and to develop effective treatments.
Protein Name: Cactin, Spliceosome C Complex Subunit
Functions: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (PubMed:28062851). Required for the splicing of CDCA5/Sororin, a regulator of sister chromatid cohesion (PubMed:28062851). Involved in the regulation of innate immune response (PubMed:20829348). Acts as negative regulator of Toll-like receptor, interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling pathways (PubMed:20829348, PubMed:26363554). Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli (PubMed:20829348, PubMed:26363554)
More Common Targets
CACTIN-AS1 | CACUL1 | CACYBP | CAD | CADM1 | CADM2 | CADM3 | CADM3-AS1 | CADM4 | CADPS | CADPS2 | CAGE1 | CAHM | CALB1 | CALB2 | CALCA | CALCB | Calcium channel | Calcium release-activated channel (CRAC) | Calcium-activated chloride channel regulators | Calcium-Activated K(Ca) Potassium Channel | CALCOCO1 | CALCOCO2 | CALCR | CALCRL | CALCRL-AS1 | CALD1 | CALHM1 | CALHM2 | CALHM3 | CALHM4 | CALHM5 | CALHM6 | CALM1 | CALM2 | CALM2P1 | CALM2P2 | CALM3 | CALML3 | CALML3-AS1 | CALML4 | CALML5 | CALML6 | Calmodulin | CALN1 | Calpain | Calpain-13 | Calprotectin | CALR | CALR3 | CALU | CALY | CAMK1 | CAMK1D | CAMK1G | CAMK2A | CAMK2B | CAMK2D | CAMK2G | CAMK2N1 | CAMK2N2 | CAMK4 | CAMKK1 | CAMKK2 | CAMKMT | CAMKV | CAMLG | CAMP | cAMP Phosphodiesterase | cAMP Responsive Element Binding Protein (CREB) | cAMP-Dependent protein kinase (PKA) | CAMSAP1 | CAMSAP2 | CAMSAP3 | CAMTA1 | CAMTA2 | CAND1 | CAND1.11 | CAND2 | Cannabinoid receptor | CANT1 | CANX | Cap-binding complex | CAP1 | CAP2 | CAPG | CAPN1 | CAPN10 | CAPN10-DT | CAPN11 | CAPN12 | CAPN13 | CAPN14 | CAPN15 | CAPN2 | CAPN3 | CAPN5 | CAPN6 | CAPN7 | CAPN8