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Concept
Nuclear pore
Summary
A nuclear pore is a channel as part of the nuclear pore complex (NPC), a large protein complex found in the nuclear envelope in eukaryotic cells, enveloping the cell nucleus containing DNA, which facilitates the selective membrane transport of various molecules across the membrane.
The nuclear pore complex predominantly consists of proteins known as nucleoporins, with each NPC comprising at least 456 individual protein molecules, and 34 distinct nucleoporin proteins. About half of the nucleoporins encompass solenoid protein domains, such as alpha solenoids or beta-propeller folds, and occasionally both as separate structural domains. Conversely, the remaining nucleoporins exhibit characteristics of "natively unfolded" or intrinsically disordered proteins, characterized by high flexibility that lack ordered tertiary structure. These disordered proteins, referred to as FG nucleoporins, contain multiple phenylalanine–glycine repeats (FG repeats) in their amino acid sequences.
The principal function of nuclear pore complexes is to facilitate selective membrane transportation of various molecules across the nuclear envelope. This includes the transportation of RNA and ribosomal proteins from the nucleus to the cytoplasm, in addition to proteins (such as DNA polymerase and lamins), carbohydrates, signaling molecules, and lipids moving into the nucleus. Notably, the nuclear pore complex (NPC) can actively mediate up to 1000 translocations per complex per second. While smaller molecules can passively diffuse through the pores, larger molecules are often identified by specific signal sequences and are facilitated by nucleoporins to traverse the nuclear envelope.
Evolutionary conserved features in sequences which code for nucleoporins regulate molecular transport through the nuclear pore. Nucleoporin-mediated transport does not entail direct energy expenditure but instead relies on concentration gradients associated with the RAN cycle (Ras-related nuclear protein cycle).
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