Date published: 2025-9-18

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TRS85 Inhibitors

TRS85 inhibitors are a class of chemical compounds designed to specifically target and inhibit the function of TRS85, a component of the TRAPP (Transport Protein Particle) complex, which is involved in intracellular trafficking processes. The TRAPP complex functions as a guanine nucleotide exchange factor (GEF) that activates Rab GTPases, essential regulators of vesicular transport between various cellular compartments, such as the endoplasmic reticulum, Golgi apparatus, and endosomes. TRS85 is a key subunit of the TRAPP complex that contributes to its role in vesicle tethering and fusion, playing an important role in processes like autophagy and the regulation of membrane trafficking. Inhibiting TRS85 disrupts the assembly or function of the TRAPP complex, leading to changes in intracellular vesicle transport and the movement of proteins and other cargo within the cell.

The chemical design of TRS85 inhibitors typically focuses on blocking the specific interactions between TRS85 and other components of the TRAPP complex or interfering with its ability to bind and activate Rab GTPases. These inhibitors may be small molecules that fit into the active or binding sites of TRS85, preventing its participation in vesicle tethering and membrane fusion events. Structural studies of TRS85 provide insights into its unique molecular features, allowing for the development of inhibitors that achieve high specificity. By inhibiting TRS85, researchers aim to understand its exact role in vesicle transport pathways, autophagy, and the maintenance of intracellular trafficking networks. Studying TRS85 inhibitors helps to elucidate the complex regulation of cellular transport systems and how specific protein interactions within the TRAPP complex control the dynamics of membrane traffic and organelle function.

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