The nuclear pore complex: a comprehensive review of structure and function
Stawicki, S. Peter and Steffen, Joseph M. (2007) The nuclear pore complex: a comprehensive review of structure and function. Other thesis, University of Louisville.
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The nuclear pore complex 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) mRNA molecules, (b) proteins, and (c) ribonucleoproteins. The transport across the nuclear membrane involves ATP hydrolysis in the great majority of cases, even though certain GTP-hydrolyzing mechanisms have also been identified. The understanding of the nuclear pore complex appears crucial to our understanding of certain disease processes. For example, it has been found that certain human viruses can “trick” our cells into transporting their ribonucleoproteins into the nucleus by using signal peptides similar to the human nuclear-localizing signals. The major challenge of today’s research on the nuclear pore complex 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 nuclear pore complex. Table of contents: Introduction (page 42); Brief History of Nuclear Pore Research (46); General Description of Nuclear Pore Transport (49); Proteins Imported into Nucleus Contain Nuclear Localization Sequences (51); Structural Components of the Nuclear Pore Complex (54); Nuclear Pore Complex: Protein Transport (61); Nuclear Pore Complex: RNA and RNP Transport (68); Nuclear Pore Complex and Virology (74); Conclusions (76). Citation: 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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