V1RF5 inhibitors constitute a unique class of chemical compounds targeting the V1RF5 protein, a crucial component of the vacuolar-type H+-ATPase (V-ATPase) complex. The V-ATPase complex plays a significant role in cellular pH regulation and ion homeostasis by pumping protons across membranes, thus establishing acidic environments within organelles like lysosomes, endosomes, and the Golgi apparatus. V1RF5 is a subunit of the V1 domain of this complex, which is integral for ATP hydrolysis. This subunit interacts closely with other components of the V1 domain to facilitate the enzymatic function of the V-ATPase.
The primary action of V1RF5 inhibitors involves binding to the V1RF5 protein, thereby disrupting its interaction with other subunits of the V1 domain. This disruption impairs the ability of the V-ATPase to perform ATP hydrolysis efficiently, which in turn affects the proton pumping activity across cellular membranes. By inhibiting V1RF5, these compounds can alter the pH balance within cellular compartments and impact various processes dependent on proper proton gradients. The study of V1RF5 inhibitors provides insight into the function and regulation of the V-ATPase complex, particularly the role of the V1RF5 subunit in maintaining cellular and organellar acidity.
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