Much
of our efforts are concentrated on Nup153, a modular pore protein with multiple
roles in nucleocytoplasmic transport (Ball
& Ullman, 2005). Nup153 is comprised of 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 is dependent upon
on-going 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 and we
hope to obtain clues from an interaction
analysis.
Read all about it!