The University of Texas Medical School at Houston
Department of Microbiology and Molecular Genetics

Kevin A. Morano, Ph.D.

 

  • Professor
  • Director, New Investigator Development Program at UT Health
  • Department of Microbiology &
    Molecular Genetics
  • University of Texas-Houston Medical School
    6431 Fannin Street, MSB 1.190
    Houston, Texas 77030
  • Telephone: (713) 500-5890
    Laboratory Telephone: (713) 500-5894
    e-mail:kevin.a.morano@uth.tmc.edu

Education:

Ph.D., University of California-Davis, 1996

Postdoctoral Fellow, University of Michigan

Research Interests:

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:
  1. how heat shock is sensed and transduced to yield a genome-wide transcriptional response
  2. how protein chaperones, including the Hsp70, Hsp90 and the Hsp110 groups, function collaboratively within the cell 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 Creutzfelt-Jakob (mad cow), and other triplet-repeat type diseases including Alzheimer's, Parkinson's, and Hunginton's, are intimately linked to protein chaperone expression and function.

Selected Publications:

  • Abrams, J., Verghese, J., Gibney, P. and Morano, K.A. (2014) Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast. J. Biol. Chem. ePub Mar 26, 289:13555-13167. [abstract]
  • Abrams, J. and Morano, K.A. (2013) Coupled assays for monitoring protein refolding in Saccharomyces cerevisiae. J. Visual. Exp. (77)e50432. [abstract]
  • Naticchia, M.R., Brown, H.A., Garcia, F.J., Lamade, A.M., Justice, S.L., Herrin, R.P., Morano, K.A. and West, J.D. (2013) Bifunctional electrophiles cross-link thioredoxins with redox relay partners in cells. Chem. Res. Toxicol. 26:490-497. [abstract]
  • *Wang, Y., Gibney, P.A., West, J.D. and Morano, K.A. (2012). The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol reactive compounds. Mol. Biol. Cell, 23:3290-3298. *Chosen as an MBoC Hightlight Article. [abstract]
  • Verghese, J. and Morano, K.A. (2012) A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with robosomes. Euk. Cell, 11:1157-1003-1011. [abstract]
  • West, J.D., Wang, Y. and Morano, K.A. (2012) Small molecule activators of the heat shock response: Chemical properties, molecular targets and therapeutic promise. Chem. Res. Toxicol. 25:2036-2053. [abstract]
  • Verghese, J., Abrams, J., Wang, Y. and Morano, K.A. (2012) Biology of the heat shock response and protein chaperone: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol. Mol. Biol. Rev. 76:115-158. [abstract]
  • Morano, K.A., Grant, C.M. and Moye-Rowley, W.S. (2012) The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics. 190:1157-1195. [abstract]
  • West, J.D., Stamm, C.E., Brown, H.A., Justice, S.L. and Morano, K.A. (2011) Enhanced toxicity of the protein cross-linkers divinyl sulfone and diethyl acetylenedicarboxylate in comparison to related monofunctional electrophiles. Chem. Res. Toxicol. 24:1457-1459. [abstract].
  • Mandal, .A.K., Gibney, P.A., Nillegoda, N.B., Theodoraki, M.A., Caplan, A.J. and Morano, K.A. (2010) Hsp110 chaperones control client fate determination in the Hsp70/Hsp90 chaperone system. Mol. Biol. Cell 21:1439-1448.[abstract]
  • Tapia, H. and Morano, K.A. (2010) Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast. Mol. Biol. Cell 21: 63-72.[abstract]
  • Trott, A., West, J.D., Klaic, L., Westerheide, S.D., Silverman, R.B., Morimoto, R.I. and Morano, K.A. (2008) Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thiol-targeted molecule. Mol Biol Cell 19:1104-1112. [abstract]
  • Shaner, L., Gibney, P.A. and Morano, K.A. (2008) The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis. Curr Genet 54:1-11. [abstract]
  • Schuermann, J.P., Jiang, J., Cuellar, J., Llorca, O., Wang, L., Gimenez, L.E., Jin, S., Taylor, A.B., Demeler, B., Morano, K.A., Hart, P.J., Valpuesta, J.M., Lafer, E.M. and Sousa, R. (2008) Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell 31:232-243. [abstract]
  • Gibney, P.A., Fries, T., Bailer, S.M. and Morano, K.A. (2008) Rtr1 is the Saccharomyces cerevisiae homolog of a novel family of RNA polymerase II-binding proteins. Eukaryot Cell 7:938-948. [abstract]
  • Shaner, L. and Morano, K.A. (2007) All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity. Cell Stress Chaperones 12:1-8. [abstract]
  • Fan, Q., Park, K.W., Du, Z., Morano, K.A. and Li, L. (2007) The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion. Genetics 177:1583-1593. [abstract]
  • Shaner, L., Sousa, R., and Morano, K.A. (2006) Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry 45:15075-15084. [abstract]

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