Misfolded proteins are the cause of many human diseases. In Parkinson’s disease, shown above, insoluble aggregates of misfolded alpha-synuclein protein (indicated by the arrows) accumulate in neurons.

The Hanna Lab studies how cells destroy their own proteins. Protein degradation is crucial for two reasons. First, misfolded proteins may be toxic to cells and must be rapidly identified and destroyed. Failure to destroy toxic misfolded proteins is the underlying basis for many diseases, including most neurodegenerative diseases, including Parkinson’s, Huntington’s, and ALS. ¬†Second, by precisely controlling the levels of key regulatory proteins, protein degradation contributes to nearly every cellular process, including the cell cycle, DNA repair, protein transport, and many others.

The ubiquitin-proteasome system is the major pathway for intracellular protein degradation. Substrates fated for destruction in this pathway are labeled with the small protein ubiquitin. This ubiquitin tag then directs the substrates to an elaborate molecular machine known as the proteasome which destroys the target protein while releasing the ubiquitin tag. The Hanna lab is studying the ubiquitin-proteasome system in yeast and mammalian cells.

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