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Research Description:
Research in my lab is focused on the questions of how the nuclear pore complex works and how its assembly and disassembly are accomplished and regulated with each cell cycle. The vertebrate nuclear pore is made up of ~50 proteins, each present in multiple copies. During interphase, nuclear pore proteins coordinate traffic into and out of the nucleus and we are interested in learning how individual proteins help to orchestrate this intracellular movement. The nuclear pore is an especially intriguing molecular machine because it supports rapid and abundant traffic while maintaining specificity. Traffic between the nucleus and cytoplasm is also of interest because it is both a constitutive process as well as one that can be a key regulatory switch. In both cases, transport is vital to normal cell function and its deregulation can contribute to cellular transformation. During the mitotic phase of the cell cycle, the vertebrate nuclear pore, along with the membranes that enclose the nucleus, disassemble. We are studying the role that pore proteins play in coordinating these key events of cell division.
Research Keywords:
Nucleocytoplasmic transport, nuclear pore complex, cell cycle, RNA export, nuclear envelope breakdown, cell biology