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

  • 2011 V Foundation Scholar Award

Research Interests

  • “Fuzzy” complexes, i.e. dynamic protein complexes, in the ubiquitination pathway
  • Liquid-like protein states and their relationship to cellular bodies
  • (Non-)structure/function relationship of intrinsically disordered proteins

Selected Publications

Csizmok V, Orlicky S, Cheng J, Song J, Bah A, Delgshaie 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 Epub online Jan 3, 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 2017