Henry F. Epstein, M.D.
- Affiliations: Department of Biochemistry & Molecular Biology, Neurology, Marine Biomedical Institute, Neuroscience & Cell Biology
- Route: 0625 120G Basic Science Building (BSB)
- Tel: (409) 772-2171
- Fax: (409) 772-3381
- Epstein Lab Webpage
- Dr. Epstein's Publications since 2002
- Epstein CV
Henry F. Epstein, M.D.
About the Lab
Dr. Epstein's laboratory is studying the role of chaperone-mediated folding in regulatory mechanisms of development and disease.
Biochemical and genetic studies on the C. elegans model as well as in various fungal species have demonstrated that a novel molecular chaperone is required for the proper folding, assembly, and function of myosins and myosin-like protein motors. The chaperone protein, named UNC-45 after the canonical gene in C. elegans, binds the well-known molecular chaperone Hsp90 as well as myosin. In mice and humans, two UNC-45-like genes are present and encode closely related but distinct isoforms. One isoform is present in many cell types and appears necessary for cell division and membrane fusion; the other isoform is expressed predominantly in heart and skeletal muscle and is necessary for sarcomere organization. The UNC-45 mammalian homologues may prove to be important targets for genetic and pharmacological intervention in certain cancers and heart failure.
Landsverk, M.L., Li, S., Hutagalung A.H., Najafov, A., Hoppe, T., Barral, J.M. and Epstein, H.F. The UNC-45 Chaperone Mediates Sarcomere Assembly through Myosin Degradation in C. elegans. J. Cell Biol. 177:205-210, 2007.
Guo, W., Chen, D., Fan, Z., and Epstein, H.F. Differential turnover of myosin chaperone UNC-45A isoforms increases in metastatic human breast cancer. J. Mol Biol.
Ni, W., Hutagalung, A.H., Li, S. and Epstein, H.F. The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegans. J. Cell Sci. 124:3164-3173, 2011.
Benian G.M. and Epstein H.F. Caenorhabditis elegans muscle: a genetic and molecular model for protein interactions in the heart. Circ Res. 109:1082-1095, 2011.
Chen, D., Li, S., Singh, R., Spinette, S., Sedlmeier, R. and Epstein, H.F. Dual function of the UNC-45b Chaperone with myosin and GATA4 in cardiac development. J. Cell Sci (in press).
Kaiser, C.M., Bujalowski, P.J., Ma, L., Anderson, J., Epstein, H.F., & Oberhauser A.F. Tracking UNC-45 Chaperone-Myosin Interaction with a Titin Mechanical Reporter. Biophys J (in press).
Link to my publications on pubmed (in addition to the one on the sidebar):