Fields of Research
- Gene Architecture and Action
- Intracellular Signaling
- Molecular Basis of Disease
- Protein Structure
Regulation of nuclear functions by ubiquitin and ubiquitin-like modifications.
The Gardner lab has a broad scope that focuses on how ubiquitin and ubiquitin-like protein modifiers regulate protein function in the nucleus. Main projects converge on elucidating the mechanisms of ubiquitin-mediated misfolded protein degradation in nuclear protein quality control, understanding the functions of ubiquitination in regulating ribosome biogenesis at the level of ribosomal rDNA transcription and ribosome assembly, and uncovering novel roles of protein sumoylation in response to cellular stress.
We welcome new thoughts and new ideas! Come join us!!
Awards and Honors
Heather Borror (Research Scientist I)
Amanda Bradley (grad student)
Timothy Mackie (postdoc)
Nicole Marsh (grad student)
Kevin Thornton (grad student)
Oeser, M. L., Amen, T., Nadel, C. M., Bradley, A.I., Reed, B. J., Jones, R. D., Gopalan, J., Kaganovich, D., and R. G. Gardner. 2016. Dynamic sumoylation of a conserved transcription corepressor prevents persistent inclusion formation during hyperosmotic stress. PLoS Genetics 12: e1005809. http://www.ncbi.nlm.nih.gov/pubmed/26800527
Richardson, L. A., Reed, B. J., Charette, M. J., Freed, E. F., Fredrickson, E. K., Locke, M. N., Baserga, S. J., and R. G. Gardner. 2012. A conserved deubiquitinating enzyme controls cell growth by regulating RNA polymerase I stability. Cell Reports 2: 372-385. http://www.ncbi.nlm.nih.gov/pubmed/22902402
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. http://www.ncbi.nlm.nih.gov/pubmed/21211726
Gardner, R. G., Nelson, Z. W., and D. E. Gottschling. 2005. Degradation-mediated protein quality control in the nucleus. Cell 120: 803-815. http://www.ncbi.nlm.nih.gov/pubmed/15797381
Gardner, R. G., Nelson, Z. W., and D. E. Gottschling. 2005. Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin. Molecular and Cellular Biology 25: 6123-6139. http://www.ncbi.nlm.nih.gov/pubmed/15988024