This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. All nuclear processes in eukaryotic cells depend on the receptor-mediated import of proteins across the nuclear envelope from the cytoplasm where they are synthesized. A protein carrying a classical nuclear localization signal (NLS) is recognized by an importin-alpha adaptor and targeted by importin-beta to the nuclear pore complex for transit into the nucleus. However, the consensus sequences of NLSs are not sufficient to predict the nuclear localization of a protein from its amino acid sequence. The regulation of nuclear protein import is essential for many cellular processes. This regulation can be exerted at several levels, including the abundance of transport adaptors and/or receptors. In multi-cellular organisms, there are several importin-alpha family members that are differentially expressed, but the physiological relevance of their tissue specific expression and the identity of their cargo remain largely unknown. This information is critical for understanding the specialized functions of the importin-alpha family of proteins in the regulation of nucleocytoplasmic transport. In budding yeast there is a single importin-alpha gene, but in fission yeast there are two, which we have found have both common and unique roles. This makes S. pombe an ideal system in which to combine genetic, proteomic, and computational approaches to investigate the specialized roles of importin-alpha isoforms in the regulation of nucleocytoplasmic transport.
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