Kevin A. Morano, Ph.D.
- Roger J. Bulger, MD Distinguished Professor
- University of Texas Distinguished Teaching Professor
- Associate Dean for Faculty Affairs
- Associate Vice-President for Faculty Affairs and Development (UTHealth)
Dr. Morano is a native Californian who received his B.S. in Biological Sciences at the University of California, Irvine working with Drs. Stephen Weller and Ann Sakai on the evolution of dioecy in flowering plants, and his Ph.D. in Microbiology at the University of California, Davis with Dr. Daniel Klionsky studying vacuolar protein sorting and autophagy. He became interested in protein homeostasis and stress gene expression as a postdoctoral fellow at the University of Michigan with Dr. Dennis Thiele.
Dr. Morano is a recipient of the GSBS John P. McGovern Teaching Award (2007, 2013), the GSBS Paul E. Darlington Mentor Award (2013), the UT Regents’ Outstanding Teacher Award (2014), and is a Fellow of the American Association for the Advancement of Science.
- Postdoctoral Fellow
- University of Michigan
- University of California-Davis, 1996
Protein chaperones and stress response in Saccharomyces cerevisiae
The heat shock response is highly conserved in all kingdoms, making it one of the most ancient cellular regulatory systems.
We have two primary interests:
- how heat shock is sensed and transduced to yield a genome-wide transcriptional response
- how protein chaperones, including the Hsp70, Hsp90 and the Hsp110 groups, function collaboratively to maintain cellular protein homeostasis during normal growth and during adaptation to environmental stress
The baker’s yeast, Saccharomyces cerevisiae, is an ideal microbial model system in which to investigate these questions, due to its facile genetics, genomics and ease of manipulation. These studies will directly impact our understanding of how human cells respond to pathophysiological states such as cancer and anoxia which strongly induce a heat shock response. In addition, there is growing evidence that the amyloid diseases of protein misfolding, including prion-based maladies such as Creutzfeldt-Jakob (mad cow), and other triplet-repeat type disorders such as Alzheimer’s, Parkinson’s, and Huntington’s Diseases, are intimately linked to protein chaperone expression and function.
Peffer S, Goncalves, D and Morano KA (2019) Regulation of the Hsf1-dependent transcriptome via conserved bipartite contacts with Hsp70 promotes survival in yeast. J. Biol. Chem. 294(32):12191-12202.
Ford AE, Denicourt C and Morano KA (2019) Thiol stress-dependent aggregation of the glycolytic enzyme triose phosphate isomerase in yeast and human cells. Mol. Biol. Cell 30(5):554-565.
Yakubu UM and Morano KA (2018) Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding. Biol. Chem. June 1, ePub doi: 10.1515/hsz-2018-0209.
Garcia VM, Nillegoda, N, Bukau B and Morano KA (2017) Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities. Mol. Biol. Cell 28(15):2066-2075.
Peffer S, Cope K, and Morano KA (2015) Unraveling protein misfolding diseases using model systems. Future Sci. OA: 10.4155/FSO.15.41.