Name: Maureen A. Powers, Ph.D. Title: Associate Professor Cell Biology Email: email@example.com Phone: 4047278859
Address:213 Cell Biology Bldg , GA
Structure and function of the nuclear pore.
The focus of the research in my laboratory is the nuclear pore complex, the immense structure which mediates highly selective, bi-directional transport between the nucleus and cytoplasm. Recent work from ourselves and others indicates that the nuclear pore is integrated with virtually all functions of the nucleus, at all stages of the cell cycle. We take multiple approaches to address the various roles of the nuclear pore. 1. Using GFP-fusion proteins in living cells together with confocal microscopy and photobleaching, we demonstrated that the nuclear pore is an unexpectedly dynamic structure. Several of the component proteins or nucleoporins move rapidly in and out of the complex. We have shown that this mobility requires ongoing transcription and we are currently studying how the dynamics of the pore are linked to RNA transcription and export. 2. We use extracts from the eggs of Xenopus frogs that can form nuclei in vitro. By removal or modification of nuclear pore components in these extracts, we can study how individual nucleoporins are involved in nuclear assembly or other cell cycle dependent nuclear processes. 3. Another aspect of the lab is the structural analysis of nuclear pore proteins. In collaboration with Alec Hodel, we determined the first structure of a domain of a nuclear pore protein, Nup98, and we continue to extend this work to other domains of Nup98 as well as other nuclear pore proteins. 4. Nup98, a nucleoporin we have studied extensively, is a partner in chromosomal translocations found in Acute Myelogenous Leukemia. We are using cell biology, biochemistry and genomic approaches to understand how alteration of this nucleoporin leads to the development of leukemia.