Pete Douglas, Ph.D.

Post-doctoral Fellow
 
Research
I received my Bachelor’s degree in Biochemistry from the University of Colorado in Boulder and my Ph.D. from the University of North Carolina in Chapel Hill.  As a graduate student in Doug Cyr’s lab, I utilized yeast as a model system to examine mechanisms by which molecular chaperones detoxify meta-stable, aggregation-prone proteins. Chaperones conventionally act as a first line of defense against proteotoxicity by preventing aggregation of disease-linked proteins.  However, we demonstrated that chaperones can also drive assembly of unstable proteins into tightly-ordered, protective aggregates. 
 
In the Dillin lab, I examine protein homeostasis and stress response as a function of age in C. elegans.  A general decline in proteostasis network components typically accompanies age and renders the organism incapable of buffering protein misfolding events.  Furthermore, environmental stresses can further challenge proteostasis networks and accelerate age-related proteotoxicity.  I utilize worms to define novel stress response pathways which can modulate protein stability and protect against environmental insults.
 
Publications
  • Douglas PM, Dillin A. Protein homeostasis and aging in neurodegeneration.  J Cell Biol, 2010. Sep 6; 190(5):719-29.
  • Douglas PM, Cyr DM.  Interplay between protein homeostasis networks in protein aggregation and proteotoxicity.Biopolymers, 2010. Mar; 93(3):229-36.
  • Douglas PM, Summers DW, Ren HY and Cyr DM.  Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Mol Biol Cell, 2009. Oct 20; (19): 4162-73.
  • Summers DW, Douglas PM, and Cyr DM.  Roles of molecular chaperones in yeast prion formation and propagation. Prion, 2009. Apr 3; (2): 59-64.
  • Douglas PM, Summers DW and Cyr DM.  Molecular chaperones antagonize proteotoxicity by differenetially modulating protein aggregation pathways. Prion, 2009. Apr 3; (2): 51-8.
  • Summers DW, Douglas PM, Ramos CH and Cyr DM. Polypeptide transfer from Hsp40 and Hsp70 molecular chaperones. Trends Biochem Sci, 2009. May 34; (5): 230-3.
  • Summers DW, Douglas PM, Ren HY and Cyr DM. The Type I Hsp40 Ydj1 utilizes a farnesyl moiety and zinc finger-like region to suppress prion toxicity. J Biol Chem, 2009. Feb 6; 284(6): 3628-39.
  • Douglas PM, Treusch S, Ren HY, Halfmann R, Duennwald ML, Lindquist S and Cyr DM.  Chaperone-dependent amyloid assembly protects cells from prion toxicity.  Proc Natl Acad Sci, 2008. May 20; 105(20): 7206-11.