Shannon M. Doyle, Ph.D.

Staff Scientist
Laboratory of Molecular Biology

Team Member of:

Sue Wickner, Ph.D.

The Wickner lab is focused on understanding the mechanisms of ATP dependent molecular chaperones. One specific aim is to understand the role of the molecular chaperone ClpB in protein disaggregation and remodeling. We are interested in determining the biochemical mechanism of action for ClpB as well as understanding how ClpB collaborates with other chaperones, such as DnaK, in protein disaggregation.

Areas of Expertise

molecular chaperones

Contact Info

Shannon M. Doyle, Ph.D.
Center for Cancer Research
National Cancer Institute
Building 37, Room 5144
Bethesda, MD 20892-4263
Ph: 240-760-7836
doyles@mail.nih.gov
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The Wickner lab is focused on understanding the mechanisms of ATP dependent molecular chaperones. One specific aim is to understand the role of the molecular chaperone ClpB in protein disaggregation and remodeling. We are interested in determining the biochemical mechanism of action for ClpB as well as understanding how ClpB collaborates with other chaperones, such as DnaK, in protein disaggregation.

Selected Publications

  1. Protein rescue from aggregates by powerful molecular chaperone machines.
    Doyle SM, Genest O, Wickner S.
    Nat. Rev. Mol. Cell Biol.. 14: 617-29, 2013. [ Journal Article ]
  2. DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.
    Doyle SM, Hoskins JR, Wickner S.
    J. Biol. Chem.. 287: 28470-9, 2012. [ Journal Article ]
  3. Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.
    Zhang T, Ploetz EA, Nagy M, Doyle SM, Wickner S, Smith PE, Zolkiewski M.
    Proteins. 80: 2758-68, 2012. [ Journal Article ]
  4. E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly.
    Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR.
    Prion. 5: 2011. [ Journal Article ]
  5. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling.
    Genest O, Hoskins JR, Camberg JL, Doyle SM, Wickner S.
    Proceedings of the National Academy of Sciences of the United States of America. 2011. [ Journal Article ]

Shannon Doyle did her undergraduate work in Microbiology at Michigan State University. She completed her Ph.D. in Biochemistry at the University of Connecticut in the lab of Dr. Carolyn M. Teschke. She continued as a postdoctoral fellow and then research fellow with Dr. Sue Wickner in the Laboratory of Molecular Biology in the National Cancer Institute prior to becoming the lab staff scientist.