ATP13A2 activators are a group of chemicals that enhance the function of the ATP13A2 protein, also known as PARK9, which is a type of P-type ATPase believed to be involved in the active transport of polyamines, cations, and other substrates across membranes. ATP13A2 has been associated with the maintenance of lysosomal and mitochondrial integrity, playing a role in the cellular degradation pathways and ion homeostasis.
Direct activators of ATP13A2 typically increase the protein's ATPase activity, which is essential for its function as a transporter. They may bind to the ATP-binding sites of the protein, stabilizing conformations that are more efficient in hydrolyzing ATP, the energy source that drives the transport mechanism. Alternatively, these activators might interact with other regulatory domains of ATP13A2 to enhance its substrate affinity or to facilitate the proper localization of the protein within the cell, thereby increasing its functional activity. Indirect activators of ATP13A2 may work by influencing the expression of the ATP13A2 gene, leading to increased protein synthesis. They might also modulate the protein's activity by affecting the lipid composition of the lysosomal membrane, which can alter the optimal environment for ATP13A2 function. Additionally, indirect activators could influence post-translational modifications of the protein, such as phosphorylation or ubiquitination, which may be critical for its activation and stability.
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