Heather L. True, PhD
David English Smith Professor, Department of Cell Biology and Physiology
- Phone: 314-362-3934
- Email: heather.true@wustl.edu
Research Interests
Protein misfolding and aggregation are the hallmark of several neurodegenerative diseases and other disorders. Protein misfolding can be sporadic or due to genetic mutations that alter folding. In addition, chaperones that normally assist in protein folding have been linked to inherited diseases (chaperonopathies) when mutated. My research investigates how the process of protein misfolding occurs, how it propagates, and how these problems can be corrected in the cell. We are specifically interested in prions, toxic protein aggregates and amyloid associated with neurodegenerative diseases, and chaperone mutants linked to a form of muscular dystrophy. We use a yeast model system and biochemical approaches to uncover important cellular contributors and elucidate mechanisms to prevent or rescue protein misfolding and aggregation.
Professional Education
- BS: University of Wisconsin – Parkside, Kenosha, WI, 1992, Molecular Biology
- MS: University of Illinois, Urbana, IL, 1995, Microbiology
- PhD: University of Illinois, Urbana, IL, 1998, Microbiology
- Postdoc: The University of Chicago, Chicago, IL, 1998-2001, Genetics
- Postdoc: The Whitehead Institute/MIT, Cambridge, MA, 2001-2003, Genetics
Graduate & Fellowship Program Affiliations
Publications
Loss of function variants in DNAJB4 cause a myopathy with early respiratory failure (Links to an external site)
Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors (Links to an external site)
Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain (Links to an external site)
Pullen MY, Weihl CC, and True HL