Lila M. Gierasch

University of Massachusetts at Amherst


Primary Section: 21, Biochemistry
Secondary Section: 29, Biophysics and Computational Biology
Membership Type: Member (elected 2019)

Biosketch

Lila Gierasch is a biophysical chemist recognized for her work on protein folding, with particular emphasis on in vivo folding and roles of molecular chaperones. Born in Massachusetts, Gierasch graduated from Mount Holyoke College in 1970 with a degree in chemistry and obtained her Ph.D. in Biophysics from Harvard University in 1975. She held faculty positions at Amherst College, the University of Delaware, and the University of Texas Southwestern Medical School prior to joining the University of Massachusetts Amherst where she is currently Distinguished Professor of Biochemistry & Molecular Biology and Chemistry. In 2006, she received a NIH Director's Pioneer Award. Among her other honors are Sloan and Guggenheim Fellowships, the Vincent du Vigneaud and Merrifield Awards of the American Peptide Society, a D.Sc. Honoris Causa from Mount Holyoke College, the Garvan-Olin Medal and Ralph Hirschmann Award of the American Chemical Society, the Dorothy Hodgkin Award of the Protein Society, and the Mildred Cohn Award of the American Society of Biochemistry & Molecular Biology. Gierasch is Editor-in-Chief of the Journal of Biological Chemistry, a past President and a Fellow of the Biophysical Society, and a member of both the American Academy of Arts and Sciences and the National Academy of Sciences.

Research Interests

Lila Gierasch's laboratory has made fundamental contributions to the relationship between amino acid sequence and the preferred conformations of peptides and proteins. Her work shed light on turn propensities in proteins and offered a basis for design of analogues of bioactive peptides. Her lab has addressed protein folding in cells, developing tools to study the fate of newly synthesized proteins, including their proper folding and cellular localization. Her lab elucidated conformational propensities and physical properties of signal sequences, which helps to explain how diverse sequences can target a polypeptide chain to the secretory pathway. Gierasch and coworkers were involved in studies that demonstrated the roles of molecular chaperones, a network of species that protect incompletely folded proteins in the cell from aggregation and misfolding. Her lab described how molecular chaperones recognize 'unfoldedness' in their protein substrates, showing that chaperonins like GroEL exploit hydrophobic surfaces to recognize substrates, while Hsp70s bind polypeptides as extended chains. Recently, Lila Gierasch's laboratory has unraveled the allosteric mechanism of Hsp70 chaperones, which are central hubs in protein homeostasis and quality control. The work of her laboratory provides insights into the pathologies that arise from mistakes in protein folding, such as the neurodegenerative diseases.

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