The Cyr laboratory is hiring students, post-docs and technicians to conduct research funded by the National Institutes of Health and the Cystic Fibrosis Foundation.

We are focused on understanding the protein folding problem and defining cellular responses to proteotoxic stress. A central focus is understanding how Hsp70 molecular chaperones mediate protein triage and determine the fate of misfolded proteins. Answers to this question explain mechanisms for protein misfolding disease and identify treatments.

Ongoing projects are in the following areas:

1. Mechanisms for specification of Hsp70 function by J-domain proteins.

2. Study of mechanisms by which the DNAJB12/Hsp70 complex triage Cystic Fibrosis causing CFTR mutants for premature degradation by the proteasome or lysosome.

3. Evaluation of how ER-associated molecular chaperones suppress the dominant toxicity of retinitis pigmentosa causing rhodopsin mutants.

4. Study of how defects in the folding/assembly of lung surfactant complexes cause proteotoxicity in the secretory pathway and fatal onset of lung fibrosis.

Links: Cyr Lab Publications from 1985 to present: >
Google Scholar Citations of Cyr Lab Publications: