Katharine S. Ullman, PhD
- Breast Cancer
- Cancer Biomarkers
- Cell Division
- Nuclear Pore Complex
- Departments: Biochemistry - Adjunct Professor, Oncological Sciences - Professor
- Cancer Center Programs: Cell Response & Regulation
Academic Office Information
Huntsman Cancer Institute
2000 Circle of Hope, Room: 5345
Salt Lake City, UT 84112
Huntsman Cancer Institute (HCI) investigator Katharine Ullman, PhD, is a professor in the Department of Oncological Sciences at the University of Utah School of Medicine, an adjunct professor in the Department of Biochemistry at the University of Utah, and a member of the Cell Response and Regulation Program. She began serving as the Associate Dean of the Graduate School at the University of Utah in 2016.
Ullman and her research team focus on the coordination of cell division, with a particular interest in how disassembly and assembly of nuclear architecture is integrated with other events of cell division. The nucleus harbors a specialized environment, optimized to protect and regulate the cell's DNA. Mis-coordination of cellular remodeling during division leaves the DNA vulnerable to damage and mis-regulation. Elucidating this aspect of cell cycle control opens a new avenue to understanding cell function and how mistakes in division may contribute to tumorigenesis.
Ullman earned a PhD from Stanford University before going to the University of California at San Diego for her postdoctoral studies, which were funded in part by the American Cancer Society. She is a recipient of a Burroughs Wellcome Career Award in the Biomedical Sciences and a Scholar award from the Leukemia and Lymphoma Society.
|Postdoctoral Training||University of California at San Diego
In the Laboratory of Dr. Douglass Forbes
|Doctoral Training||Stanford University
Microbiology & Immunology
Biochemistry, Molecular Biology & Cell Biology
- Gu M, LaJoie D, Chen OS, von Appen A, Ladinsky MS, Redd MJ, Nikolova L, Bjorkman PJ, Sundquist WI, Ullman KS, Frost A (2017). LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells. Proc Natl Acad Sci U S A, 114(11), E2166-E2175.
- Mackay DR, Howa AC, Werner TL, Ullman KS (2017). Nup153 and Nup50 promote recruitment of 53BP1 to DNA repair foci by antagonizing BRCA1-dependent events. J Cell Sci, 130(19), 3347-3359.
- Mackay DR, Ullman KS (2015). ATR and a Chk1-Aurora B pathway coordinate postmitotic genome surveillance with cytokinetic abscission. Mol Biol Cell, 26(12), 2217-26.
- Sundquist WI, Ullman KS (2015). CELL BIOLOGY. An ESCRT to seal the envelope. Science, 348(6241), 1314-5.
- Fay MM, Clegg JM, Uchida KA, Powers MA, Ullman KS (2014). Enhanced arginine methylation of programmed cell death 4 protein during nutrient deprivation promotes tumor cell viability. J Biol Chem, 289(25), 17541-52.
- Chow KH, Elgort S, Dasso M, Powers MA, Ullman KS (2014). The SUMO proteases SENP1 and SENP2 play a critical role in nucleoporin homeostasis and nuclear pore complex function. Mol Biol Cell, 25(1), 160-8.
- Makise M, Mackay DR, Elgort S, Shankaran SS, Adam SA, Ullman KS (2012). The Nup153-Nup50 protein interface and its role in nuclear import. J Biol Chem, 287(46), 38515-22.
- Chow KH, Factor RE, Ullman KS (2012). The nuclear envelope environment and its cancer connections. Nat Rev Cancer, 12(3), 196-209.
- Mackay DR, Ullman KS (2011). Coordinating postmitotic nuclear pore complex assembly with abscission timing. Nucleus, 2(4).
- Powers MA, Fay MM, Factor RE, Welm AL, Ullman KS (2011). Protein arginine methyltransferase 5 accelerates tumor growth by arginine methylation of the tumor suppressor programmed cell death 4. Cancer Res, 71(16), 5579-87.
- Mackay DR, Makise M, Ullman KS (2010). Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint. J Cell Biol, 191(5), 923-31.
- Mackay DR, Elgort SW, Ullman KS (2009). The nucleoporin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis. Mol Biol Cell, 20(6), 1652-60.
- Liu J, Prunuske AJ, Fager AM, Ullman KS (2003). The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Dev Cell, 5(3), 487-98.