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REVIEW ARTICLE: REPUBLICATION
Year : 2017  |  Volume : 3  |  Issue : 3  |  Page : 24-38

The nuclear pore complex: A comprehensive review of structure and function


Department of Biology, College of Arts and Sciences, University of Louisville, Louisville, KY, USA

Correspondence Address:
Stanislaw P Stawicki
Department of Research and Innovation, St. Luke's University Health Network, EW2 Research Administration, 801, Ostrum Street, Bethlehem, PA 18015
USA
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/IJAM.IJAM_26_17

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The nuclear pore complex (NPC) is an important functional entity of every eukaryotic cell's nuclear membrane. It enables selective transport of materials across the nuclear membrane in an organized and orderly fashion. Substances carried in and out of the nucleus by the NPC include three major groups of molecules: (a) Messenger ribonucleic acid molecules, (b) proteins, and (c) ribonucleoproteins (RNPs). The transport across the nuclear membrane involves adenosine triphosphate hydrolysis in the great majority of cases even though certain guanosine triphosphate-hydrolyzing mechanisms have also been identified. The understanding of the NPC appears crucial to our understanding of certain pathological processes. For example, it has been found that certain human viruses can “trick” our cells into transporting their RNPs into the nucleus using signal peptides similar to the human nuclear-localizing signals. The major challenge of today's research on the NPC resides in identification of over one hundred of its distinct polypeptide units and in determining their functions and interactions. To date, many of the structural proteins involved in the NPC have been identified, but the mechanism of their interactions still remains largely hypothetical. This project discusses the structure and function of the NPC. The following core competencies are addressed in this article: Medical knowledge. Republished with permission from: Stawicki SP, Steffen JM. The nuclear pore complex: A comprehensive review of structure and function. OPUS 12 Scientist 2007;1(2):39-87.


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