COPG 抑制因子

The COPI (Coat Protein Complex I) coat complex is an integral component of the intracellular transport machinery, particularly involved in retrograde transport between the Golgi apparatus and the endoplasmic reticulum. This sophisticated protein assembly facilitates the formation of transport vesicles, aiding in the shuttling of lipids and proteins between cellular compartments. The function of the COPI complex is paramount in ensuring the proper sorting and distribution of these molecular constituents within the cell, a process vital for maintaining cellular homeostasis and function. Seven coat proteins have been identified, representing subunits of the "coatomer" complex. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP.

COPI coat complex Inhibitors are molecules designed to interfere with the normal operation of this transport system. These inhibitors can act at various stages of the COPI-mediated transport process. Some might directly interact with COPI subunits, preventing their proper assembly or recruitment to membranes. Others could target upstream regulators, such as the ArfGEFs, which play a crucial role in initiating COPI coat formation by activating small G proteins essential for the process. Examples of such inhibitors include Golgicide A, which inhibits the ArfGEF GBF1, and Brefeldin A, a fungal metabolite that disrupts ADP-ribosylation factor (Arf) GEFs' function. It's crucial to understand that while these compounds have been invaluable tools in deciphering the intricacies of intracellular transport pathways, their mode of action can be multifaceted. Interference with the COPI complex can have broad cellular consequences, given the fundamental role of this protein assembly in maintaining intracellular traffic and organelle integrity.