SUCLG2: A Potential Drug Target and Biomarker for Diseases (G8801)

Target Name: SUCLG2

NCBI ID: G8801

SUCLG2: A Potential Drug Target and Biomarker for Diseases

SUCLG2 (stimulated Ubiquitin-Proteasome Ligation), also known as GTPSCS (G protein-coupled Ubiquitin-Proteasome System), is a protein that plays a crucial role in cellular signaling and autophagy. Extensive research has identified SUCLG2 as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

The SUCLG2 protein is a 21-kDa transmembrane protein that belongs to the G protein-coupled Ubiquitin-Proteasome System (GUPS). This system is responsible for the degradation of misfolded or damaged proteins, as well as the regulation of protein homeostasis and cell signaling pathways. SUCLG2 is composed of a catalytic center with a nucleotide-binding oligomerization domain (NBO), a carboxylic acid terminal, and a cytoplasmic tail.

SUCLG2 functions as a negative regulator of the GUPS, ensuring that misfolded or damaged proteins are targeted for degradation and that properly processed proteins are retained for protein homeostasis. The NBO domain of SUCLG2 is critical for its function, as it enables the formation of a covalent complex with a specific nucleotide. This nucleotide-binding oligomerization is the first step in the process of SUCLG2-mediated protein degradation, and it is essential for the efficient removal of damaged or misfolded proteins.

SUCLG2 has been implicated in various cellular processes, including cell signaling, DNA replication, and cellular stress response. SUCLG2 has been shown to play a crucial role in the regulation of the ubiquitinylation (U-tail) and ubiquitination (U-tagging) of various proteins , including target proteins for various signaling pathways, such as the TOR signaling pathway, the PI3K/AKT signaling pathway, and the NF-kappa-B signaling pathway.

In cancer, SUCLG2 has been implicated in the regulation of cell cycle progression, apoptosis, and angiogenesis. SUCLG2 has been shown to promote the G1/S transition and the G2/M transition in cell cycle, which are critical for the development and progression of cancer. Additionally, SUCLG2 has been linked to the regulation of cell apoptosis, as it has been shown to play a role in the execution of programmed cell death (PCD) in response to various stimuli, including chemotherapy drugs.

In neurodegenerative diseases, SUCLG2 has been shown to contribute to the pathogenesis of various neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease. SUCLG2 has been shown to participate in the regulation of the translation of mutated genes, as well as the maintenance of cellular homeostasis in the presence of neurodegenerative hallmarks.

In autoimmune disorders, SUCLG2 has been implicated in the regulation of immune cell function and the development of autoimmune diseases. SUCLG2 has been shown to play a role in the regulation of T cell proliferation, differentiation, and clonal expansion, as well as in the regulation of the production of antibodies.

In conclusion, SUCLG2 is a highly conserved protein that has been implicated in various cellular processes and functions, including cell signaling, protein homeostasis, cell cycle progression, apoptosis, and neurodegenerative diseases. Because of its potential as a drug target and biomarker, SUCLG2 is a promising target for the development of new therapies for various diseases.

Protein Name: Succinate-CoA Ligase GDP-forming Subunit Beta

Functions: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit

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