Unlocking the Potential of ATPase Class I Type 8A Member 1 as a Drug Target and Biomarker

Target Name: ATP8A1

NCBI ID: G10396

ATP8A1

Unlocking the Potential of ATPase Class I Type 8A Member 1 as a Drug Target and Biomarker

Introduction

ATP (adenosine triphosphate) is the primary energy source for all cell types, and its levels play a crucial role in regulating various cellular processes. ATPase is the most well-known protein involved in ATP synthesis and degradation. In particular, ATPase class I type 8A member 1 (ATPase1) is a critical enzyme involved in the regulation of ATP levels and functions. ATPase1 has been identified as a potential drug target and biomarker due to its unique structure, function, and expression patterns.

Structure and Function

ATPase1 is a 26kDa protein that consists of an N-terminal alpha-helices, a catalytic domain, and a C-terminal T-loop. The N-terminal and C-terminal regions contain conserved nucleotide-binding oligomerization (NBO) domains, which are involved in nucleotide recognition and hydrolysis. The catalytic domain is responsible for the critical catalytic functions of ATPase1, including ATP binding, hydrolysis, and release.

ATPase1 functions as the ATP synthase enzyme, which means it catalyzes the synthesis of ATP from ADP and phosphate. The synthesis of ATP from ADP and phosphate via ATPase1 is a critical process for cellular energy homeostasis. ATPase1 activity can be inhibited by various chemical inhibitors, such as sildenafil and efavirenz, which are commonly used in the treatment of erectile dysfunction and HIV/AIDS, respectively.

Expression and Localization

ATPase1 is highly expressed in various tissues, including heart, brain, and kidney. Its expression is also sensitive to various factors, such as temperature, pH, and processing conditions, which may impact its catalytic efficiency and stability.

ATPase1 is predominantly localized to the cytoplasm of cells, with a relatively high localization in the endoplasmic reticulum (ER) and a low expression in the nuclear envelope (NE). The localization of ATPase1 in the ER is consistent with its functions as an ATP synthase enzyme. The ER is a site of intense protein synthesis, including ATP synthase, and is known as the protein synthesis machine (PSM).

Drug Sensitivity and Inhibition

Several studies have investigated the drug sensitivity of ATPase1 and its potential as a drug target. Sildenafil, a commonly used treatment for erectile dysfunction, has been shown to inhibit the activity of ATPase1, leading to a decrease in the levels of ATP available for the synthesis of new ATP. Similarly, efavirenz, another HIV/AIDS treatment, has also been shown to inhibit the activity of ATPase1, which may contribute to its anti-retroviral effects.

In addition to inhibiting ATPase1 function, sildenafil and efavirenz have been shown to alter the expression levels of ATPase1. For instance, sildenafil has been shown to downregulate the expression of ATPase1 in the PC12 cells, while efavirenz has been shown to increase the expression of ATPase1 in the T471 cells.

Biomarker Potential

The potential use of ATPase1 as a biomarker or drug target has been evaluated in various models. One approach is to use ATPase1 as a target for small molecules that can modulate its catalytic activity or stability. Since ATPase1 is sensitive to inhibitors, small molecules that can inhibit its activity or stability may be identified as potential therapeutic compounds.

One such example is the molecule N-Acetyl-L-Tyrosine (NAT), which is a natural compound that has been shown to modulate the activity of various enzymes, including ATPases. NAT has been shown to inhibit the activity of

Protein Name: ATPase Phospholipid Transporting 8A1

Functions: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:31416931). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:31416931). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane (By similarity). Acts as aminophospholipid translocase at the plasma membrane in neuronal cells (By similarity)

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