Kravats Lab

Research Interests

Proteins play an important role in all biological processes. In order for proteins to function properly, they must fold into their correct three dimensional conformation and localize to the correct subcellular compartment within the crowded cellular environment. Protein misfolding can be linked to most diseases and is caused by errors in protein synthesis, mutations, protein misfolding and cellular stresses. Molecular chaperones are important for maintaining protein quality control within the cell. They assist in protein folding, protein remodeling and targeting proteins for degradation.

The Kravats Lab is interested in protein remodeling mechanisms by molecular chaperones located in the endoplasmic reticulum (ER). One of the most abundant ER chaperones is Grp94, an Hsp90 paralog. Numerous client proteins and cochaperones have been identified for Hsp90 and its role in protein remodeling has become better understood in recent years. However, Grp94 has a limited number of client proteins, no identified cochaperones and a far less understood mechanistic role in how it functions. Our lab uses a combination of biochemical, biophysical and computational approaches to elucidate the mechanistic action of Grp94 and how it participates in ER protein quality control. We are also interested in understanding client protein selection by Grp94 and the collaboration of Grp94 with other ER chaperones and cochaperones in client protein remodeling.