Tanja Mittag, PhD
Tanja Mittag, PhD

Tanja Mittag, PhD

Assistant Member, St. Jude Faculty

Departments

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

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: June 2015