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Mittag Lab: About Us

Function of intrinsically disordered proteins (IDPs) and “fuzzy” complexes

The Mittag lab studies the function of intrinsically disordered proteins (IDPs) in cell signaling. IDPs, which do not adopt unique, well-folded structures, are ubiquitous in all kingdoms of life and most common in multi-cellular eukaryotes. More than 30% of all human proteins, 79% of all cancer-associated proteins and many proteins associated with neurodegenerative diseases have long disordered regions.

IDPs are highly enriched in signaling processes and appear to have key functions in mediating protein interactions. However, our understanding of the underlying molecular processes is still very limited. The Mittag lab is interested in elucidating the physiological functions of disorder, and determining why dynamic and disordered protein complexes are often more beneficial than stably folded complexes in signal transduction.

Current projects in the lab focus on:

  • “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

We recently received an R01 grant from NIGMS to investigate the role of multivalency in SPOP-mediated ubiquitination.

Improving our understanding of the function of IDPs may provide opportunities to develop drugs that specifically target these proteins, potentially leading to novel therapeutics for cancer and neurodegenerative disease.

Methodology: Biophysical tools combined with biochemistry and cell biology

We use a combination of biophysical, biochemical and cell biological approaches to characterize IDPs and correlate their properties with their biological functions. Our primary biophysical tools include NMR spectroscopy, light scattering, fluorescence approaches and analytical ultracentrifugation.

Read more at Mittag Lab: Research.