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Tanja Mittag, PhD
Tanja Mittag, PhD

Tanja Mittag, PhD

Associate Member, St. Jude Faculty



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

  • Liquid-liquid phase separation and its link to functional compartmentalization
  • Dysregulation of phase separation in cancer and neurodegenerative diseases
  • Sequence/conformation/function relationship of intrinsically disordered proteins

Selected Publications

Bremer A, Mittag T*, Heymann M*. Microfluidic characterization of macromolecular liquid-liquid phase separation. Lab Chip 20(22):4225-4234, 2020.

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.

Borcherds W, Bremer A, Borgia MB, Mittag T. How do intrinsically disordered protein regions encode a driving force for liquid-liquid phase separation? Curr Opin Struct Biol 67:41-50, 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.

Martin EW, Hopkins JB, Mittag T. Small angle x-ray scattering experiments of monodisperse samples close to the solubility limit. arXiv 2020.

Gomes GNW, Krzeminski M, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC. Integrating multiple experimental data to determine conformational ensembles of an intrinsically disordered protein. BioRxiv 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.

Kumar P, Agarwal PK, Waddell BM, Mittag T, Serpersu EH, Cuneo MJ. Low-Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad. Angew. Chem. Int. Ed. Engl. 58 (45): 16260-16266, 2019.

Peran I, Mittag T. Molecular structure in biomolecular condensates. Curr Opin Struct Biol 60:17-26, 2019.

Cuneo M, Mittag T. The ubiquitin ligase adaptor SPOP in cancer, FEBS J 286(20):3946-3958, 2019.

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.

Mittag T*, Parker R*. Multiple modes of protein-protein interactions promote RNP granule assembly. J Mol Biol 430(23):4636-4649, 2018. 

Martin EW*, Mittag T*. The relationship of sequence and phase separation in protein low-complexity regions. Biochemistry 57(17):2478-2487, 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.

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.

Csizmok V, Orlicky S, Cheng J, Song J, Bah A, Delgoshaie N, Lin H, Mittag T, Sicheri F, Chan HS, Tyers M, Forman-Kay JD. An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase. Nat Commun 8:13943, 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. 

Marzahn M, Marada S, Lee J, Nourse S, Kenrick S, Zhao H, Ben-Nissan G, Kolaitis RM, Peters JL, Pounds S, Errington WJ, Prive GG, Taylor JP, Sharon M, Schuck P, Ogden SK*, Mittag T*. Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles. EMBO J 35(190):1254-75, 2016. Cover article.

Pierce WK, Grace CR, Lee J, Nourse A, Marzahn MR, Watson ER, High AA, Peng J, Schulman BA, Mittag T. Multiple weak linear motifs enhance recruitment and processivity in SPOP-mediated substrate ubiquitination. J Mol Biol 428(6): 1256-71, 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.

Feige MJ, Behnke J, Mittag T, Hendershot LM. Dimerization-dependent Folding Underlies Assembly Control of the Clonotypic αβT cell Receptor Chains J Biol Chem 290: 26821-31, 2015.

Nourse A, Mittag T. The cytoplasmic domain of the T-cell receptor zeta subunit does not form disordered dimers. J Mol Biol 426:62-70, 2014.

Forman-Kay JD, Mittag T. From sequence and forces to structure, function, and evolution of intrinsically disordered proteins. Structure 21:1492-1499, 2013.

Duda D, Olszewski J, Tron AE, Hammel M, Lambert LJ, Waddell MB, Mittag T, DeCaprio JA, Schulman BA. Structure of a Glomulin-RBX1-Cul1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Mol Cell 47:371-382, 2012. (Comment in Mol Cell 47:331-332, 2012.)

Tang X, Orlicky S, Mittag T, Pawson T, Csizmok V, Forman-Kay JD, Sicheri F, Tyers M. Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase. Proc Natl Acad Sci USA 109, 3287-3292, 2012.

Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. Structure-function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 18:494-506, 2010. (Preview: Konrat R. The meandering of disordered proteins in conformational space. Structure 18:416-419, 2010.)

Mittag T, Kay LE, Forman-Kay JD. Protein dynamics and conformational disorder in molecular recognition. J Mol Recognit 23:105-116, 2010.

Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. Dynamic equilibrium engagement of a polyvalent ligand with a single site receptor. Proc Natl Acad Sci USA 105:17772-17777, 2008.

Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, Chan HS. Poly-electrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad. Sci USA 104:9650-9655, 2007.

Mittag T, Forman-Kay JD. Atomic-level characterization of disordered protein ensembles. Curr Op Struct Biol 17:3-14, 2007.

Mittag T, Franzoni L, Cavazzini D, Schaffhausen B, Rossi GL, Günther U. Retinol modulates site-specific mobility of apo-cellular retinol-binding protein to promote ligand binding. J Am Chem Soc128:9844-9848, 2006.

Koglin A, Mofid MR, Löhr F, Schäfer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dötsch V. Conformational switches modulate protein interactions in peptide antibiotic synthetases.Science 312:273-276, 2006.

Mittag T, Schaffhausen B, Günther U. Tracing kinetic intermediates during ligand binding. J Am Chem Soc 126:9017-9023, 2004.

Mittag T, Schaffhausen B, Günther U. Direct observation of protein ligand interaction kinetics.Biochemistry 42:11128-11136, 2003.

Günther U, Mittag T, Schaffhausen B. Probing Src Homology 2 domain ligand interactions by differential line broadening. Biochemistry 41:11658-11669, 2002.

Weber T, Schaffhausen B, Liu Y, Günther U. NMR structure of the N-SH2 domain of the p85 subunit of Phosphatidylinositide 3-Kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site. Biochemistry 39:15860-15869, 2000.

Last update: January 2021