Nuclear pore complex

The nuclear pore complex is a large assembly of proteins embedded in the nuclear envelope. It selectively transports molecules between the nucleus and cytoplasm while allowing small molecules to diffuse through.

Nucleoporin: A protein that forms part of the nuclear pore complex or helps regulate transport through it. Nucleoporins build the pore’s scaffold and create the selective barrier inside its channel.
Nuclear envelope: A double membrane that encloses the eukaryotic cell nucleus and separates it from the cytoplasm. Nuclear pore complexes span both membranes of this enclosing structure.
mRNA export: The movement of messenger RNA from the nucleus to the cytoplasm for translation. Newly processed mRNA exits the nucleus through pore complexes.
Nuclear pore complex assembly: The process by which nucleoporins build and insert nuclear pore complexes into the nuclear envelope. Assembly explains how pores form in an envelope whose membranes remain intact.
Selective permeability: The property of allowing some substances to cross a barrier more readily than others. The physical basis of the pore’s selectivity remains an active subject of study.
Phenylalanine-glycine repeat: A short sequence motif rich in phenylalanine and glycine, found in many nucleoporins. FG repeats form a flexible barrier that transport receptors can cross.
Nuclear lamina: A meshwork of proteins lining the inner nuclear membrane and supporting nuclear shape and organization. The lamina anchors and organizes pores at the nuclear envelope.
Ribosome biogenesis: The cellular production and assembly of ribosomal subunits from ribosomal RNA and proteins. Ribosomal subunits assembled in the nucleus must pass through pores to reach the cytoplasm.
Nuclear pore complex evolution: The evolutionary history of nuclear pore complexes and their constituent proteins across eukaryotes. Comparisons across species reveal both ancient architecture and substantial structural variation.
Nuclear pore complex structure: The three-dimensional organization of proteins and membranes that make up a nuclear pore complex. Structural models continue to refine the arrangement of its many components.

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