Michael Rosen (UT, Southwestern Medical Ctr.) Webinar

Michael Rosen (UT, Southwestern Medical Ctr.) Webinar

Butler Seminar Series

Event Date/Location

October 7, 2020 - 12:00 pm to 1:00 pm
Thomas Laboratory


  • Michael Rosen

    Professor and Mar Nell and F. Andrew Bell Distinguished Chair
    University of Texas, Southwestern

    Dr. Rosen is the Chair of the Department of Biophysics at UT Southwestern Medical Center and an Investigator of the Howard Hughes Medical Institute.  Dr. Rosen received undergraduate degrees in chemistry and in chemical engineering from the University of Michigan in 1987.  He then spent a year in Alan Battersby’s lab in the Department of Chemistry at the University of Cambridge as a Winston Churchill Foundation Scholar.  He received his Ph.D. in Chemistry from Harvard University in 1993 under the direction of Stuart Schreiber, where he studied the structure and function of the FK506 binding protein, FKBP12.  He was a Damon Runyon-Walter Winchell post-doctoral fellow in the laboratories of Tony Pawson and Lewis Kay at the University of Toronto, where he studied regulation of the signaling adaptor protein, Crk, and developed methods of selective methyl group labeling of proteins for NMR spectroscopy.  Dr. Rosen started his independent laboratory in 1996 in the Cellular Biochemistry and Biophysics Program at the Memorial Sloan-Kettering Cancer Center in New York City, and moved to UTSW in 2001. 


Cellular Organization Through Liquid-Liquid Phase Separation

Biomolecular condensates are two- and three-dimensional compartments in eukaryotic cells that concentrate specific collections of proteins and nucleic acids without an encapsulating membrane.  Many condensates behave as dynamic liquids, and are believed to form through liquid-liquid phase separation (LLPS) driven by interactions between multivalent macromolecules.  In my talk I will discuss a new direction in the lab focused on understanding how multivalent interactions among nucleosomes may afford organization and dynamic regulation of chromatin through LLPS.  These behaviors may contribute to formation of functionally distinct compartments in the eukaryotic nucleus, which are important to processes including gene regulation and DNA repair.  If time permits, I will also discuss our ongoing work to understand how the macroscopic properties of natural, many-component condensates arise from the physical properties and interactions of their constituents.


Free and open to the university community and the public.


Sabine Petry, Department of Molecular Biology