Richard Gardner, PhD
Associate Professor, Pharmacology
Research in the Gardner lab is focused on understanding how ubiquitin and ubiquitin-like modifiers affect key nuclear processes such as the degradation of misfolded proteins and prevention of aggregation, ribosome biogenesis, and responses to stress – all of which can impact lifespan and the aging process if mismanaged.
Honors and awards
2009 – New Scholar in Aging Award, Ellison Medical Foundation
2008 – Kimmel Scholar Award, Sidney Kimmel Foundation for Cancer Research
2008 – Marian E. Smith Junior Faculty Research Award, University of Washington
Gallagher PS, Clowes Candadai SV, Gardner RG. Gardner. (2014). The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility. Journal of Cell Science, 127: 1980-1991. 127 (Pt 9):1980-91.
Fredrickson EK, Clowes Candadai SV, Tam CH, Gardner RG. (2013). Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction. Molecular Biology of the Cell, 24: 1041-1052.
Fredrickson EK, Gallagher PS, Clowes Candadai SV, Gardner RG. (2013). Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility. Journal of Biological Chemistry, 288: 6130-6139.
Richardson LA, Reed BJ, Charette JM, Freed EF, Fredrickson EK, Locke MN, Baserga SJ, Gardner RG. (2012). A conserved deubiquitinating enzyme controls cell growth by regulating RNA polymerase I stability. Cell Reports, 2: 372-385.
Rosenbaum, J. C., Fredrickson, E. K., Oeser, M. L., Garrett-Engele, C. M., Locke, M. N., Richardson, L. A., Nelson, Z. W., Hetrick, E. D., Milac, T. I., Gottschling, D. E., and R. G. Gardner. 2011. Disorder targets misorder in nuclear quality control degradation: an intrinsically disordered ubiquitin ligase directly recognizes misfolded substrates. Molecular Cell 41: 93-106.