This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The nucleus of the cell is of central importance to an organism. It serves to store and organize genetic material, while separating and protecting this very important information from the host of other cellular components. While the nucleus requires this protective isolation, it also needs to communicate with the rest of the cell, exchanging proteins and RNA, for a variety of nuclear and cytoplasmic processes which act in concert. The nuclear pore complex (NPC) is the gatekeeper of the nucleus. It is an immense assembly of proteins, perhaps the largest protein structure in eukaryotic cells [1], embedded in the nuclear envelope. Because of its large size, however, pointed experimental study has been difficult, and as a result, the mechanism by which the NPC selectively allows good material across the nuclear envelope, while preventing the transit of the bad , remains unknown. It is known, however, that in order to cross the nuclear envelope, a large molecule must first associate with a transport receptor protein (reviewed in [2, 3, 4, 1, 5, 6]). It is hypothesized that so-called FG-repeat proteins in the NPC recognize the transport receptor and allow the complex to pass. Understanding precisely how this recognition occurs is vital to determining how the NPC protects the nucleus.
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