Target Name: PCK1
NCBI ID: G5105
Review Report on PCK1 Target / Biomarker Content of Review Report on PCK1 Target / Biomarker
PCK1
Other Name(s): PCKGC_HUMAN | phosphoenolpyruvate carboxykinase 1 | serine-protein kinase PCK1 | PEPCK-C | MGC22652 | PEPCK1 | Phosphoenolpyruvate carboxykinase 1 | phosphoenolpyruvate carboxykinase, cytosolic | phosphopyruvate carboxylase | Phosphoenolpyruvate carboxykinase, cytosolic [GTP] | phosphoenolpyruvate carboxykinase 1 (soluble) | Serine-protein kinase PCK1 | PEP carboxykinase | Phosphoenolpyruvate carboxykinase, cytosolic [GTP] | phosphoenolpyruvate carboxylase | Phosphopyruvate carboxylase | PCKDC | PEPCKC

PCK1: A Potential Drug Target and Biomarker

Proteasome-conversion kinase (PCK) is a protein that plays a crucial role in the regulation of protein degradation in cells. It is a widely expressed protein that is involved in various cellular processes, including cell signaling, DNA replication, and protein-protein interactions. One of the PCKs is PCK1 (PCKGC_HUMAN), which is a protein that is expressed in various tissues of the human body. In this article, we will discuss PCK1 and its potential as a drug target or biomarker.

Structure and Function

PCK1 is a 22 kDa protein that is composed of 115 amino acid residues. It has a unique structure that consists of a catalytic core and a regulatory domain. The catalytic core is composed of a Rossmann-fold, a deep groove, and a hyperbolic loop, which are responsible for the protein's catalytic activity. The regulatory domain is composed of a nucleotide-binding domain and a scaffold domain. The nucleotide-binding domain is responsible for interacting with nucleotides, while the scaffold domain is responsible for maintaining the protein's stability.

PCK1 is involved in the regulation of protein degradation by activating the ubiquitin-proteasome system (UPS). This system is responsible for the degradation of damaged or unnecessary proteins, and it is a crucial regulatory system that helps to maintain the cell's homeostasis. PCK1 plays a key role in the activation of the UPS by recognizing and interacting with the ubiquitin protein.

PCK1 is also involved in the regulation of DNA replication and cell signaling. It has been shown to play a role in the regulation of mitosis, meiosis, and DNA replication. In addition, PCK1 has been shown to be involved in cell signaling by regulating various signaling pathways, including the TGF-β pathway.

Drug Target Potential

PCK1 has been identified as a potential drug target due to its various functions in the cell. One of the reasons for its potential as a drug target is its involvement in the regulation of protein degradation, which is a crucial aspect of cellular signaling. By targeting PCK1, researchers may be able to manipulate the activity of this protein and achieve a variety of cellular effects.

Another reason for PCK1's potential as a drug target is its involvement in the regulation of DNA replication and cell signaling. By targeting PCK1, researchers may be able to manipulate these processes and achieve a variety of cellular effects.

Biomarker Potential

PCK1 has also been identified as a potential biomarker for various diseases. For example, PCK1 has been shown to be involved in the regulation of cancer cell growth and has been used as a potential biomarker for cancer. In addition, PCK1 has been shown to be involved in the regulation of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. By targeting PCK1, researchers may be able to develop new treatments for these diseases.

Conclusion

In conclusion, PCK1 is a protein that is involved in various cellular processes, including cell signaling, DNA replication, and protein-protein interactions. It has a unique structure and function, and it plays a crucial role in the regulation of cellular processes. As a result, PCK1 has been identified as a potential drug target and biomarker. Further research is needed to fully understand the role of PCK1 in the regulation of cellular processes and to develop new treatments based on its properties.

Protein Name: Phosphoenolpyruvate Carboxykinase 1

Functions: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:30193097, PubMed:24863970, PubMed:26971250, PubMed:28216384). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed:30193097, PubMed:24863970, PubMed:26971250, PubMed:28216384). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:30193097). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (PubMed:32322062). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (PubMed:32322062)

The "PCK1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PCK1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   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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PCK2 | PCLAF | PCLO | PCM1 | PCMT1 | PCMTD1 | PCMTD1-DT | PCMTD2 | PCNA | PCNA-AS1 | PCNAP1 | PCNAP3 | PCNP | PCNPP1 | PCNT | PCNX1 | PCNX2 | PCNX3 | PCNX4 | PCOLCE | PCOLCE-AS1 | PCOLCE2 | PCOTH | PCP2 | PCP4 | PCP4L1 | PCSK1 | PCSK1N | PCSK2 | PCSK4 | PCSK5 | PCSK6 | PCSK6-AS1 | PCSK7 | PCSK9 | PCTP | PCYOX1 | PCYOX1L | PCYT1A | PCYT1B | PCYT2 | PDAP1 | PDC | PDCD1 | PDCD10 | PDCD11 | PDCD1LG2 | PDCD2 | PDCD2L | PDCD4 | PDCD4-AS1 | PDCD5 | PDCD6 | PDCD6IP | PDCD6IPP2 | PDCD6P1 | PDCD7 | PDCL | PDCL2 | PDCL3 | PDCL3P4 | PDCL3P6 | PDE10A | PDE11A | PDE11A-AS1 | PDE12 | PDE1A | PDE1B | PDE1C | PDE2A | PDE2A-AS1 | PDE3A | PDE3B | PDE4A | PDE4B | PDE4C | PDE4D | PDE4DIP | PDE5A | PDE6A | PDE6B | PDE6C | PDE6D | PDE6G | PDE6H | PDE7A | PDE7B | PDE7B-AS1 | PDE8A | PDE8B | PDE9A | PDE9A-AS1 | PDF | PDGFA | PDGFA-DT | PDGFB | PDGFC | PDGFD | PDGFRA | PDGFRB