Skip to main content
Tanja Mittag, PhD
Tanja Mittag, PhD


Diploma – Johann Wolfgang Goethe University, Frankfurt, Germany (2001)
PhD – Johann Wolfgang Goethe University, Frankfurt, Germany (2004)
Postdoctoral Training – The Hospital for Sick Children, Toronto, Ontario, Canada

Honors & Awards

  • 1999-2000 German National Academic Foundation Fellowship          
  • 2001-2004 Graduate Fellowship, German National Academic Foundation
  • 2005-2008 Post Ph.D. Research Fellowship, National Cancer Institute of Canada (NCIC) and Terry Fox Foundation
  • 2009 Postdoctoral Research Award, IDP Subgroup of the Biophysical Society
  • 2011 V Foundation Scholar Award
  • 2021 Michael and Kate Bárány Award of the Biophysical Society

Research Interests

  • Phase separation and its role in functional compartmentalization 
  • Dysregulation of phase separation in cancer and neurodegenerative diseases
  • Sequence/conformation/function relationship of intrinsically disordered proteins

Selected Publications

Farag M, Borcherds WM, Bremer A, Mittag T*, Pappu RV*. Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions. Nat Commun Sep 8;14(1):5527, 2023. doi: 10.1038/s41467-023-41274-x. PMID: 37684240 (*co-corresponding author)

Mayr C, Mittag T, Tang TD, Wen W, Zhang H, Zhang H. Frontiers in biomolecular condensate research. Nat Cell Biol Apr;25(4):512-514, 2023. doi: 10.1038/s41556-023-01102-2. PMID: 36973422

Cuneo MJ, O'Flynn BG, Lo, Y-H, Sabri N, Mittag T. Higher-order SPOP assembly reveals a basis for cancer mutant dysregulation. Mol Cell Jan 14, 2023. doi: 10.1016/j.molcel.2022.12.033

Mittag T*, Pappu RV*. A conceptual framework for understanding phase separation and addressing open questions and challenges. Mol Cell 82: 2201-2214, 2022.

Bremer A#, Farag M#, Borcherds WM#, Peran I, Martin EW, Pappu RV*, Mittag T*.  Deciphering how naturally occurring sequence features impact the phase behaviors of disordered prion-like domains. Nat Chemistry 13: 196-207, 2022.

Martin EW, Harmon TS, Hopkins JB, Chakravarthy S, Incicco J, Schuck P, Soranno A, Mittag T. A multi-step nucleation process determines the kinetics of prion-like domain phase separation. Nat Commun. 12(1):4513, 2021.

Martin EW#, Thomasen FE#, Milkovic NM#, Cuneo MJ, Grace CR, Nourse A, Lindorff-Larsen K*, Mittag T*. Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation. Nucleic Acids Res 49(5): 2931-2945, 2021.

Zeng X, Holehouse AS, Mittag T, Chilkoti A, Pappu RV. Connecting coil-to-globule transitions to full phase diagrams for intrinsically disordered proteins. Biophys J 119 (2):402-418, 2020.

Yang P*, Mathieu C*, Kolaitis RM, Zhang P, Messing J, Yurtsever U, Yang Z, Wu J, Li Y, Pan Q, Yu J, Martin EW, Mittag T, Kim HJ, Taylor JP. G3BP1 is a tunable switch that triggers phase separation to assemble stress granules. Cell 181:325-345, 2020.

Martin EW#, Holehouse AS#, Peran I#, Farag M, Incicco JJ, Bremer A, Grace CR, Soranno A, Pappu RV*, Mittag T*. Valence and patterning of aromatic residues determine the phase behavior of disordered prion-like domains. Science 367(6478):694-699, 2020.

Schmit JD*, Bouchard JJ, Martin EW, Mittag T. Protein network structure enables switching between liquid and gel states. JACS 142(2):874-883, 2020.

Bouchard JJ, Otero JH, Scott DC, Szulc EM, Martin EW, Sabri N, Granata D, Marzahn MR, Lindorff-Larsen K, Salvatella X, Schulman BA, Mittag T. Cancer mutations of the tumor suppressor SPOP disrupt the formation of active, phase-separated compartments. Mol Cell 72:19-36, 2018.

Boeynaems S, Alberti S, Fawzi NL, Mittag T, Parker R, Polymenidou M, Rousseau F, Schymkowitz J, Shorter J, Taylor JP, Wolozin B, Van Den Bosch L, Tompa P, Fuxreiter M. Protein phase separation: a new phase in cell biology. Trends in Cell Biol 28:420-435, 2018.

A. Wang, A.E. Conicella, H.B. Schmidt, E.W. Martin, S.N. Rhoads, A.N. Reeb, A. Nourse, D. Ramirez Montero, V.H. Ryan, R. Rohatgi, F. Shewmaker, M.T Naik, T. Mittag, Y.M. Ayala, N.L. Fawzi. A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation and RNA splicing. EMBO J 37(5):pii: e97452, 2018.

Alberti S*, Gladfelter A*, Mittag T*. Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates. Cell 176(3): 419-434, 2019.

Mackenzie IR, Nicholson AM, Sarkar M, Messing J, Pottier C, Annu K, Baker M, Perkerson RB, Kurti A, Matchett BJ, Mittag T, Perkerson E, Hsiung GYR, Krieger C, Murray ME, Kato M, Fryer JD, Petrucelli L, Zinman L, Weintraub S, Mesulam M, Keith J, Zivkovic SA, Roos RP, Zuchner S, Graff-Radford NR, Petersen RC, Caselli RJ, Wszolek ZK, Finger E, Lippa C, Dickson DW, Lacomis D, Stewart H, Kim HJ, Rogaeva E, Bigio E, Boylan KB, Taylor JP, Rademakers R. Mutations in the stress granule protein TIA1 in amyotrophic lateral sclerosis and frontotemporal dementia. Neuron. 95: 808-816, 2017.

Martin EW, Holehouse A, Grace CR, Hughes A, Pappu RV*, Mittag T*. Sequence determinants of the conformational properties of an intrinsically disordered protein prior to and upon multisite phosphorylation. J Am Chem Soc 138(47):15323-15335, 2016. 

Molliex A, Temirov J, Lee J, Coughlin M, Kanagaraj AP, Kim HJ, Mittag T*, Taylor JP*. Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization. Cell 163(1): 123-33, 2015.

Last update: November 2023