Eileen M. Lafer, PhD, Professor
|Education:||BA in Biochemistry, Chemistry, and Biology from Brandeis University, 1978.|
PhD in Biochemistry from Tufts University Sackler School of Biomedical Sciences, 1983.
|Post Doctoral:||Massachusetts Institute of Technology, 1983-1986.|
|Other Faculty Positions:||Assistant - Associate Professor w tenure, University of Pittsburgh, 1986-1994.|
My lab studies the molecular machines involved in vesicular traffic, a fundamental process utilized by all compartmentalized cells from yeast to man to move proteins between different membranous compartments. Our initial interest in this subject grew out of our efforts to dissect the molecular mechanisms underlying synaptic transmission. We showed that the clathrin pathway is essential for synaptic vesicle recycling. We went on to characterize the mechanisms of clathrin polymerization and uncoating that underlie this process. The uncoating reaction is promoted by the chaperone protein Hsc70, which is a member of the Hsp70 family of chaperone proteins. These chaperone proteins are also involved in many aging related disorders that are a consequence of the accumulation of damaged, aggregated proteins (Alzheimer's, ALS, Parkinson's, Huntington's, and others). Therefore we are also interested in understanding the roles these chaperones play in both protein aggregation diseases and cancer during the aging process. We utilize a combination of biochemical and physiological approaches including solution biochemistry (surface plasmon resonance, dynamic light scattering, analytical ultracentrifugation, nuclear magnetic resonance spectroscopy), X-ray crystallography, and electrophysiology. Our work has broad significance since chaperones are involved in many macromolecular complex remodeling reactions.
- Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly.
Zhuo Y, Ilangovan U, Schirf V, Demeler B, Sousa R, Hinck AP, Lafer EM
J Mol Biol: 2010-11-26; 404(2); 274-90 Epub: 2010-09-25.
PMID: 20875424   LINK:
- ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.
Woo HJ, Jiang J, Lafer EM, Sousa R
Biochemistry: 2009-12-08; 48(48); 11470-7
PMID: 19883127   LINK:
- Structure of the Hsp110:Hsc70 nucleotide exchange machine.
Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, Hart PJ, Valpuesta JM, Lafer EM, Sousa R
Mol Cell: 2008-07-25; 31(2); 232-43 Epub: 2008-06-12.
PMID: 18550409   LINK:
- Structural basis of J cochaperone binding and regulation of Hsp70.
Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R
Mol Cell: 2007-11-09; 28(3); 422-33
PMID: 17996706   LINK:
- Keep the traffic moving: mechanism of the Hsp70 motor.
Sousa R, Lafer EM
Traffic: 2006-12-01; 7(12); 1596-603 Epub: 2006-10-06.
PMID: 17026666   LINK:
Complete Publication Listing