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How Are Proteins Transported Out Of The Nucleus?

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How are proteins transported out of the nucleus?
Eukaryotic cells rely majorly on the aqueous pores of the nuclear envelope, the double membrane system surrounds the nucleoplasm, as a pathway for transportation of proteins between the nucleus and the cytosol. The process is commonly known as a kind of gated transportation as to the fact that the nuclear pore complexes (NPC) that are embedded in the aqueous pores serve as gates that only select certain molecules to pass.

Proteins, as macromolecules, cannot directly diffuse through the pathway of NPCs due to the presence of the disordered region of channel nucleoporins; the bundles of the channel nucleoporins are compactly aligned in disarray in the central pore, and certain phenylalanine-glycine (FG) repeats, which are present on the bundles, are believed to associate via low-affinity, cohesive interactions to form a permeability barrier of the pore (Xu & Powers, 2013) and stop macromolecules to pass through freely, thus it requires energy input and aids from other molecules to traffic proteins through NPCs.

Proteins that are needed to move out of the nucleus are often referred as cargos; these proteins have a specific part of their amino acid sequences, nuclear export signals, that contains information to lead the protein to their desired destination, which is the cytosol. Proteins with their corresponding signals can be recognized by and bonded to a soluble protein, nuclear export receptors (Nakielny et al. 1999); these

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