Target Name: ATP6V1G2
NCBI ID: G534
Review Report on ATP6V1G2 Target / Biomarker Content of Review Report on ATP6V1G2 Target / Biomarker
ATP6V1G2
Other Name(s): ATP6V1G2 variant 1 | ATP6G | ATPase H+ transporting V1 subunit G2 | V-type proton ATPase subunit G 2 (isoform a) | ATPase, H+ transporting, lysosomal (vacuolar proton pump) | ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2 | V-ATPase 13 kDa subunit 2 | V-type proton ATPase subunit G 2 | ATPase H+ transporting V1 subunit G2, transcript variant 1 | ATP6G2 | NG38 | V-ATPase subunit G 2 | vacuolar proton pump G subunit 2 | VMA10 | VATG2_HUMAN | Vacuolar proton pump subunit G 2 | H(+)-transporting two-sector ATPase, subunit G2 | vacuolar ATP synthase subunit G 2

Exploring the Potential Drug Target ATP6V1G2: Unlocking the Power of ATP in Cancer Treatment

ATP (adenosine triphosphate) is a ubiquitous molecule that plays a critical role in various cellular processes. It is the energy currency of the cell and has been linked to numerous physiological functions. One of the ATP-dependent processes that has received increasing attention in recent years is the regulation of cell survival and division. When cell division goes awry, cancerous cells can arise, and these rogue cells can eventually form tumors. In order to combat this disease, researchers have been investigating various ATP-related molecules, with the goal of finding potential drug targets. In this article, we will focus on one such target: ATP6V1G2.

The ATP6V1G2 Molecule

ATP6V1G2 is a protein that is expressed in various cell types, including neurons, muscle cells, and cancer cells. It is a key regulator of the cell's energy metabolism and is involved in the production of ATP, which is the primary energy source for the cell. ATP6V1G2 is composed of several subunits that work together to ensure its stability and function.

One of the most significant subunits of ATP6V1G2 is the catalytic subunit, which is responsible for catalyzing the conversion of ATP into ADP. This process, known as ATP hydrolysis, is a critical step in the production of ATP and is rate-limiting for the overall ATP production. The catalytic subunit is known for its unique structure, which includes a Rossmann-fold, a specific type of hydrophobic pocket that allows it to interact with other molecules.

In recent years, researchers have been investigating the potential clinical applications of ATP6V1G2 as a drug target. One of the main reasons for this interest is the molecule's ability to interact with various drug molecules, including small molecules, peptides, and antibodies. This interactivity makes it an attractive target for researchers to develop new treatments for various diseases.

ATP6V1G2 in Cancer

The role of ATP6V1G2 in cancer is still being fully understood, but research has shown that it is involved in various cellular processes that promote tumor growth. For example, studies have suggested that ATP6V1G2 may be involved in the regulation of cell adhesion, a process that is critical for the development of cancerous tumors. Additionally, the molecule has been implicated in the regulation of cell proliferation, which is a key factor in the development of many types of cancer.

In addition to its role in cell proliferation, ATP6V1G2 has also been shown to contribute to the development of cancer by promoting the formation of blood-vessel-dependent tumors. This is because ATP6V1G2 has been shown to regulate the formation of blood vessels in the Developing Mouse Embryo (DMEG) model, a widely used model for studying cancer development.

Targeting ATP6V1G2

The potential drug target that is most closely related to ATP6V1G2 is the molecule's catalytic subunit. This subunit is the site of many of the known interactions with small molecules, peptides, and antibodies that have been shown to interact with ATP6V1G2. As a result, drugs that target the catalytic subunit of ATP6V1G2 have the potential to inhibit its function and slow down or stop the growth of cancer cells.

One of the most promising strategies for targeting the catalytic subunit of ATP6V1G2 is the use of small molecules that can inhibit the activity of ATP6V1G2's catalytic subunit. For example, a recent study identified a small molecule called KU-8878 that inhibits the activity of the catalytic subunit with high affinity. The results showed that treatment with KU-8878 significantly reduced the growth of cancer cells, suggesting that it has the potential to be a useful drug for the treatment of cancer.

Another approach to

Protein Name: ATPase H+ Transporting V1 Subunit G2

Functions: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment

The "ATP6V1G2 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 ATP6V1G2 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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ATP6V1G2-DDX39B | ATP6V1G3 | ATP6V1H | ATP7A | ATP7B | ATP8 | ATP8A1 | ATP8A2 | ATP8B1 | ATP8B1-AS1 | ATP8B2 | ATP8B3 | ATP8B4 | ATP8B5P | ATP9A | ATP9B | ATPAF1 | ATPAF2 | ATPase | ATPSCKMT | ATR | ATRAID | Atrial natriuretic peptide (ANP) receptor | ATRIP | ATRN | ATRNL1 | ATRX | ATXN1 | ATXN10 | ATXN1L | ATXN2 | ATXN2L | ATXN3 | ATXN3L | ATXN7 | ATXN7L1 | ATXN7L2 | ATXN7L3 | ATXN7L3B | ATXN8OS | Augmin | AUH | AUNIP | AUP1 | AURKA | AURKAIP1 | AURKAP1 | AURKB | AURKC | Aurora Kinase | AUTS2 | AVEN | AVIL | AVL9 | AVP | AVPI1 | AVPR1A | AVPR1B | AVPR2 | AWAT1 | AWAT2 | AXDND1 | AXIN1 | AXIN2 | AXL | Axonemal dynein complex | AZGP1 | AZGP1P1 | AZGP1P2 | AZI2 | AZIN1 | AZIN2 | AZU1 | B-cell Antigen Receptor Complex | B2M | B3GALNT1 | B3GALNT2 | B3GALT1 | B3GALT1-AS1 | B3GALT2 | B3GALT4 | B3GALT5 | B3GALT5-AS1 | B3GALT6 | B3GALT9 | B3GAT1 | B3GAT1-DT | B3GAT2 | B3GAT3 | B3GLCT | B3GNT2 | B3GNT3 | B3GNT4 | B3GNT5 | B3GNT6 | B3GNT7 | B3GNT8 | B3GNT9 | B3GNTL1 | B4GALNT1