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.
The Rosen lab seeks to understand the formation, regulation and functions of enigmatic, cellular compartments termed biomolecular condensates. These evolutionarily conserved structures concentrate diverse but specific groups of molecules without a surrounding membrane. Condensates appear to form through the physical process of liquid-liquid phase separation. Using a range of techniques, including biochemical reconstitution and in vitro and cellular microsopies, we investigate phase separation in both engineered and natural condensates. The former, in their simplified nature, enable precise isolation of key molecular parameters governing condensate behaviors, revealing general principles. The latter allow demonstration of these principles in more complex natural biochemical and cellular systems. Ultimately, we seek to understand cell organization on scales spanning nanometers to microns.
The Rosen lab website can be found at: www.utsouthwestern.edu/labs/rosen/
- University of Michigan-Ann Arb (1987), Chemistry
- University of Michigan-Ann Arb (1987), Chemical Engineering
- Graduate School
- Harvard University (1993), Organic Chemistry
- Biological phase separation
- cell biology of the actin cytoskeleton
- polymer physics/chemistry
- structural biology
- A composition-dependent molecular clutch between T cell signaling condensates and actin.
- Ditlev JA, Vega AR, Köster DV, Su X, Tani T, Lakoduk AM, Vale RD, Mayor S, Jaqaman K, Rosen MK, Elife 2019 Jul 8
- Regulation of Transmembrane Signaling by Phase Separation.
- Case LB, Ditlev JA, Rosen MK, Annu Rev Biophys 2019 Apr
- Stoichiometry controls activity of phase-separated clusters of actin signaling proteins.
- Case LB, Zhang X, Ditlev JA, Rosen MK, Science 2019 03 363 6431 1093-1097
- Who's in and Who's Out-Compositional Control of Biomolecular Condensates.
- Ditlev JA, Case LB, Rosen MK J. Mol. Biol. 2018 Aug
- Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites.
- Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM Cell 2018 Apr 173 3 693-705.e22
- Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly.
- Protter DSW, Rao BS, Van Treeck B, Lin Y, Mizoue L, Rosen MK, Parker R Cell Rep 2018 Feb 22 6 1401-1412
- Allosteric Modulation of Grb2 Recruitment to the Intrinsically Disordered Scaffold Protein, LAT, by Remote Site Phosphorylation.
- Huang WYC, Ditlev JA, Chiang HK, Rosen MK, Groves JT J. Am. Chem. Soc. 2017 Nov
- Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins.
- Harmon TS, Holehouse AS, Rosen MK, Pappu RV Elife 2017 Nov 6
- Rac1 GTPase activates the WAVE regulatory complex through two distinct binding sites.
- Chen B, Chou HT, Brautigam CA, Xing W, Yang S, Henry L, Doolittle LK, Walz T, Rosen MK Elife 2017 Sep 6
- Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs.
- Lin Y, Currie SL, Rosen MK J. Biol. Chem. 2017 Sep
Honors & Awards
- Allen Distinguished Investigator, a program funded through The Paul G. Allen Frontiers Group
- Emil Kaiser Award, Protein Society
- Mar Nell and F. Andrew Bell Distinguished Chair in Biochemistry
- Carolyn R. Bacon Professorship in Medical Science and Education
- Edith & Peter O’Donnell Award from the Texas Academy of Medicine, Engineering and Science
- Howard Hughes Medical Institute
- Boyer Award, Memorial Sloan-Kettering Cancer Center
- Sidney Kimmel Scholar Award
- Beckman Young Investigator
- Presidential Early Career Award for Scientists and Engineers (PECASE)
- Winston Churchill Scholar