The nuclear envelope of eukaryotic cells compartmentalizes the cytoplasm and the nucleus. Some proteins residing on the inner nuclear membrane interact with chromatin and are involved in the chromatin organization and the control of gene expression. We study how modification of these inner nuclear membrane proteins during the cell cycle might change its interaction with the chromatin and control the disassembly-assembly of the nuclear envelope. We also study the inner nuclear membrane proteins in budding yeast that undergoes closed mitosis without disassembling the nuclear envelope. We study whether mitotic modification of the nuclear membrane proteins is conserved in yeast and whether it is important for nuclear division. In addition, we are interested in the fundamental question of how the size and shape of the nuclear envelope are controlled.

真核細胞用細胞核膜將細胞區分為細胞質及細胞核，細胞核內膜經由一些蛋白質和染色體接觸，而控制染色體在細胞核內的組織及基因的表現。高等生物在進行有絲分裂時會分解細胞核膜，待染色體分離後再重新組合，這就是所謂的開放性有絲分裂。我們研究細胞核內膜的蛋白質在有絲分裂時經由何種變化來減低它和染色體的接觸，以利細胞核膜分解。單細胞生物酵母菌的細胞核膜在有絲分裂時並不會分解，我們也想知道進行這種封閉式有絲分裂的細胞核內膜蛋白質是否也有有絲分裂期的特殊變化，以及這種變化是否幫助染色體的分離或細胞核的分裂。此外，我們也研究細胞核的大小及形狀如何被控制。

Post-translational conjugation with ubiquitin targets protein for degradation through the proteasome, directs protein localization, and signals membrane trafficking. The ubiquitin-selective chaperone Cdc48, an evolutionarily conserved and abundant protein of the AAA-ATPase family, is involved in some of the ubiquitin-mediated processes. Cdc48 exerts its diverse functions through associated adaptor molecules including a family of UBX domain-containing proteins. We study how Cdc48 and its adaptors might control dynamic events in the cell cycle and ubiquitin-mediated proteolysis. We aim to understand the basic principles of Cdc48 by identifying targets of UBX proteins and their regulation by Cdc48 through the adaptors.