ATPase Phospholipid Transporting 10B: A Potential Drug Target and Biomarker

Target Name: ATP10B

NCBI ID: G23120

ATPase Phospholipid Transporting 10B: A Potential Drug Target and Biomarker

Introduction

ATP (adenylyl cyclic phosphate) is a crucial energy source for the cell and serves as the energy carrier for most cellular processes. The production and breakdown of ATP are tightly regulated, and ATPase, the enzyme responsible for ATP synthesis, is involved in this process . Phospholipids, the building blocks of cell membranes, are also involved in this process and play a crucial role in maintaining the structural integrity of the cell membrane. However, the regulation of ATPase and its interactions with phospholipids have not been well understood.

ATPase is a transmembrane protein that spans the membrane of the cell and is involved in the hydrolysis of ATP to release energy. It consists of a catalytic active site, a regulatory site, and a transmembrane region. The catalytic active site is responsible for the conversion of ATP to ADP, releasing energy in the form of a phosphate group. The regulatory site is responsible for regulating the activity of ATPase and is involved in the binding of ATP and phospholipids. The transmembrane region is responsible for maintaining the structural integrity of the protein and is involved in its expression and localization.

ATPase has been shown to play a crucial role in the regulation of various cellular processes, including cell growth, differentiation, and survival. It has also been implicated in a number of diseases, including cancer, neurodegenerative diseases, and cardiovascular disease. Therefore, the study of ATPase and its regulation is of great interest and has significant implications for the development of new therapeutic approaches.

ATPase has been shown to interact with various phospholipids, including phosphatidylcholine (PC), phosphatidylserine (PS), and phospholipid acylinositol (PM). These interactions are important for the regulation of ATPase activity and the function of the ATPase-phospholipid complex. The regulation of ATPase activity by phospholipids has been shown to play a role in various cellular processes, including cell signaling, cytoskeletal organization, and cell survival.

One of the ATPase-phospholipid interactions that has been well studied is the interaction between ATPase and PC. Studies have shown that the addition of PC to the ATPase active site can inhibit the activity of ATPase, indicating that this interaction plays a negative role in the regulation of ATPase activity.

In addition to its interaction with PC, ATPase has also been shown to interact with other phospholipids, including PS and PM. These interactions have been shown to play important roles in the regulation of ATPase activity and the function of the ATPase-phospholipid complex.

The ATPase-phospholipid complex is a critical regulatory interaction that plays a role in the regulation of various cellular processes. The regulation of ATPase activity by phospholipids has been shown to be involved in the regulation of cell signaling, cytoskeletal organization, and cell survival. Therefore , the study of ATPase and its regulation by phospholipids is of great interest and has significant implications for the development of new therapeutic approaches.

Conclusion

ATPase is a transmembrane protein that is involved in the regulation of ATP synthesis and the breakdown. It consists of a catalytic active site, a regulatory site, and a transmembrane region. The catalytic active site is responsible for the conversion of ATP to ADP, releasing energy in the form of a phosphate group. The regulatory site is responsible for regulating the activity of ATPase and is involved in the binding of ATP and phospholipids. The transmembrane region is responsible for maintaining the structural integrity of the protein and is involved in its expression and localization.

ATPase has been shown to interact with various phospholipids, including

Protein Name: ATPase Phospholipid Transporting 10B (putative)

Functions: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes. Plays an important role in the maintenance of lysosome membrane integrity and function in cortical neurons

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