Read all about it! UCSD–Nature Molecule Page
Much of our efforts are concentrated on Nup153, a modular pore protein with multiple roles in nucleocytoplasmic transport (Ball and Ullman, 2005). Nup153 comprises three distinct domains: a unique N-terminal domain, a central C2-C2 zinc finger-like region, and an FG-rich C-terminal domain. In collaboration with Ueli Aebi and Birthe Fahrenkrog at the M.E. Müller Institute in Basel, Switzerland, we have shown that domains within Nup153 are differentially exposed at the nuclear pore complex (Fahrenkrog, 2002) and that epitope exposure changes with pore activity (Paulillo et al., 2005, Paulillo et al., 2006). In addition to having a complex steady-state localization at the pore, Nup153 has been shown by fluoresence recovery after photobleaching (FRAP) to be highly dynamic (Daigle et al., 2001). With Maureen Powers' lab at Emory University, we (Eric Griffis in particular!) have found that the mobility of Nup153 depends on ongoing transcription, and we have mapped the domains needed to link Nup153 to pol I and pol II transcription (Griffis et al., 2004). Characterizing the molecular link between these regions of Nup153 and the transcription machinery will be very important.