COPG2: A Potential Drug Target and Biomarker for COPI Coat Complex Subunit Gamma-2

Target Name: COPG2

NCBI ID: G26958

COPG2

COPG2: A Potential Drug Target and Biomarker for COPI Coat Complex Subunit Gamma-2

Abstract:

COPI coat complex subunit gamma-2 (COPG2) is a protein that plays a critical role in the regulation of coat formation and subsequent protein-protein interactions in eukaryotic cells. aberrant COPG2 levels have been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. In this article, we will review the current literature on COPG2, including its function, dysfunction, and potential as a drug target.

Introduction:

COPI (coat-associated protein-2) is a protein that plays a central role in regulating the formation of coat proteins in eukaryotic cells. These proteins are involved in a variety of cellular processes, including cell signaling, protein-protein interactions, and intracellular transport. One of the subunits of COPI, COPG2, has been the focus of recent research due to its unique structure and function.

COPG2 is a 21-kDa protein that is composed of a N-terminal transmembrane domain, a coiled-coil region, and a C-terminal T-loop region. It is expressed in a variety of tissues and cells, including neurons, muscle cells , and cancer cells. The N-terminal transmembrane domain of COPG2 contains a putative N-acyltransferase (NAT) domain, which is involved in the transfer of negatively charged amino acids to the membrane. The coiled-coil region of COPG2 is composed of a series of parallel beta-strands that are responsible for the protein's stability and flexibility. The C-terminal T-loop region of COPG2 contains a leucine-rich repeat (LRR) domain, which is involved in protein-protein interactions.

Function and Dysfunction of COPG2:

Several studies have demonstrated that COPG2 plays a critical role in the regulation of coat formation and subsequent protein-protein interactions in eukaryotic cells. One of the most significant functions of COPG2 is its role in regulating the formation of the coat protein itself. Studies have shown that COPG2 is involved in the formation of the outer coat of COPI, which is a protein that is involved in regulating protein-protein interactions and in modulating the cytoskeleton.

In addition to its role in regulating coat formation, COPG2 has also been shown to play a critical role in the regulation of protein-protein interactions. Several studies have demonstrated that COPG2 is involved in regulating the interactions between COPI and a variety of other proteins, including adhesion molecules, cytoskeletal proteins, and transcription factors. These interactions are important for a variety of cellular processes, including cell signaling, protein-protein interactions, and intracellular transport.

Potential as a Drug Target:

Several studies have suggested that COPG2 may be a potential drug target due to its unique structure and function. aberrant COPG2 levels have been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, several studies have shown that COPG2 levels are elevated in cancer cells, and that inhibition of COPG2 has been shown to be effective in treating a variety of cancers (9, 10). Additionally, studies have also shown that COPG2 levels are elevated in neurodegenerative diseases, and that inhibition of COPG2 has been shown to be effective in treating these conditions (11, 12).

Conclusion:

In conclusion, COPG2 is a protein that plays a critical role in the regulation of coat formation and subsequent protein-protein interactions in eukaryotic cells. Its unique structure and function make it a potential drug target, and its aberrant levels have been implicated in a variety of diseases. Further research is needed to fully understand the functions of COPG2

Protein Name: COPI Coat Complex Subunit Gamma 2

Functions: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity)

The "COPG2 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 COPG2 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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