pore complex assembly

Definition

Target type: biologicalprocess

The aggregation, arrangement and bonding together of a set of components to form a pore complex. A pore complex is a small opening in a membrane that allows the passage of liquids and/or gases. [GOC:jl, GOC:mah]

The nuclear pore complex (NPC) is a large, intricate protein structure that spans the nuclear envelope, the double membrane that encloses the eukaryotic nucleus. It serves as the sole gateway for the transport of molecules between the nucleus and cytoplasm, playing a critical role in maintaining the integrity and functionality of the cell. The assembly of the NPC is a complex process involving multiple steps, including the initial formation of a scaffold structure, the recruitment of specific nucleoporins (proteins that constitute the NPC), and the precise arrangement of these proteins into a functional complex. The process is tightly regulated, ensuring proper assembly and the formation of a robust and selective barrier.

The assembly of the NPC begins with the formation of a scaffold structure, which serves as a foundation for the complex. This scaffold is typically formed by a specific set of nucleoporins that interact with the nuclear envelope and with each other. These nucleoporins often possess unique structural features, such as coiled-coil domains, that allow them to assemble into stable and elongated structures.

Once the scaffold is established, other nucleoporins are recruited to the complex. These nucleoporins can be broadly classified into two categories: transmembrane nucleoporins and soluble nucleoporins. Transmembrane nucleoporins are anchored to the nuclear envelope and form the structural core of the NPC. They interact with the scaffold nucleoporins and with each other to form a stable framework. Soluble nucleoporins are found within the central channel of the NPC and are involved in regulating the transport of molecules.

The assembly of the NPC is not a passive process. It is actively regulated by a complex network of interactions between nucleoporins, chaperone proteins, and other cellular factors. These interactions ensure that the NPC is assembled in a precise and ordered manner, with each nucleoporin occupying its specific location within the complex.

As the NPC assembles, it gradually acquires its characteristic shape and structure. This includes the formation of a central channel lined with soluble nucleoporins, which acts as a selective barrier for the transport of molecules. The NPC also develops a basket-like structure on the nuclear side, which serves as a docking site for nuclear transport receptors.

The assembly of the NPC is a dynamic process, with individual nucleoporins constantly exchanging and the complex undergoing constant remodeling. This dynamic nature allows the NPC to adapt to changing cellular conditions and to maintain its functionality over time.

In conclusion, the assembly of the NPC is a complex and highly orchestrated process that involves the coordinated action of multiple proteins and cellular factors. The NPC is a vital component of the eukaryotic cell, ensuring the efficient and selective transport of molecules between the nucleus and cytoplasm. Understanding the process of NPC assembly is critical for elucidating the mechanisms underlying nuclear transport and for gaining insights into the regulation of gene expression and other cellular processes.'
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Proteins (4)

Compounds (33)