Sue Jaspersen

Biography

As an undergrad at Washington D.C.’s Georgetown University, Sue Jaspersen, Ph.D., was growing weary of writing papers required for her history major. So she took on a challenge that in the end would force a rapid U-turn in her career plans. A student poll had ranked organic chemistry the hardest class on campus, so she decided to enroll in it—just to prove she could succeed. “I was majoring in history because I wanted to go to law school and work on Capitol Hill,” says Jaspersen, who hated memorizing the textbook in junior high biology so much she hadn’t even considered a science career. But after acing the organic chemistry class, she changed majors and graduated with a B.S. in chemistry in 1994. Jaspersen, whose biographical essay to graduate school included the apparently irresistible line, “I’m from Nebraska and I like basketball and cats,” chose the University of California, San Francisco (UCSF), to pursue graduate work in biochemistry. There, as a HHMI pre-doctoral fellow she studied cell cycle regulation in the yeast Saccharomyces cerevisiae in the lab of David Morgan.

Research Interest

The Nuclear Envelope: Structure and Function The hallmark feature of eukaryotic cells is their nucleus, which contains the genetic material. In addition to the chromosomes, the nucleus also contains numerous protein complexes that control gene expression, DNA replication and repair, chromosome segregation and many nuclear processes are essential for genomic integrity and cell proliferation. The core of my lab's interests lies in elucidating the structure and geography of the nucleus, especially in terms of the nuclear envelope (NE). The nuclear membrane is a double lipid bilayer. The outer nuclear membrane (ONM) is contiguous with the endoplasmic reticulum (ER) and shares a number of integral membrane components. In contrast, the inner nuclear membrane (INM) contains a distinct set of proteins and lipids, which is different from either the ONM or the ER. Proteomic analysis of the INM indicates that it is composed of at least 80 distinct proteins, most of which are uncharacterized. Mutants in genes encoding INM proteins underlie a broad spectrum of human diseases ranging from tissue specific diseases of muscle, bone and fat cells to multi-system diseases such as the premature aging syndrome progeria and cancer. However, which nuclear processes are altered and why different cell types are affected differently is not understood. Elucidating the mechanism by which INM proteins are localized and determining how they function in the three-dimensional organization of the nucleus will advance our understanding of human health and development.