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Sarah Hitchcock-DeGregori,Ph.D.


Present Title
Professor
Department of Pathology and Laboratory Medicine

Office Address:
Department of Pathology and Laboratory Medicine
Robert Wood Johnson Medical School
675 Hoes Lane
Piscataway, NJ 08854

Description of Research Interests
Regulation of muscle contraction, actin dynamics and cellular movement by the actin binding protein, tropomyosin. Bioinformatics approaches including evolutionary analysis and an evolutionary-based screen in the fission yeast are used to identify residues required for conserved tropomyosin functions. The methodologies range from biochemical and biophysical to cellular in order to address the folding, actin binding sites, structure-function relationships and cellular functions of mammalian and fission yeast isoforms of this coiled coil protein. The results will give insights into mechanisms of human myopathies cause by mutations in tropomyosin genes.

Undergraduate Education:
Smith College A.B., Zoology
1961-1965  

Graduate Education:
Wesleyan University
M.A., Biology
1965-1967

Case Western Reserve University
Ph.D., Biology
1967-1970                                    

Postdoctoral Training:
Brandeis University
Muscular Dystrophy Research Fellow with Dr. A.G. Szent-Györgyi
Department of Biology
1970-1973  

British-American Heart Association Research Fellow with Dr.Hugh E. Huxley,
MRC Laboratory of Molecular Biology
1973-1975 

Cambridge, England
NIH Special Fellowship                             
1973-1976

Selected Publications
For complete list PubMed

Barua, B., Winkelmann, D.A., White, H.C. and Hitchcock-DeGregori, S.E. 2012. Regulation of actin-myosin interaction by conserved periodic sites in tropomyosin. PNAS 2012 ; published ahead of print October 22, 2012, doi:10.1073/pnas.1212754109

Hitchcock-DeGregori, S.E
., Pamula, M.C., and Barua, B. 2011. Evolutionarily conserved surface residues
constitute actin binding sites of tropomyosin. Proc. Natl. Acad. Sci. USA . 108(25), 10150-10155. http://www.ncbi.nlm.nih.gov/pubmed/21642532

Hitchcock-DeGregori, S.E. and Singh, A. 2010. What makes tropomyosin an actin binding protein: a
perspective. J. Str. Biol. 170(2), 319-324. http://www.ncbi.nlm.nih.gov/pubmed/20036744

Singh, A., and Hitchcock-DeGregori, S.E. 2009. A peek into tropomyosin binding and unfolding on the actin
filament. PLoS ONE 4(7), e6336. http://www.ncbi.nlm.nih.gov/pubmed/19629180

Greenfield, N.J., Kotlyanskaya, L, and Hitchcock-DeGregori, S.E. 2009. Structure of the N terminus of a
non-muscle alpha tropomyosin in complex with the C terminus: implications for actin binding. Biochemistry
48(6), 1272-83. http://www.ncbi.nlm.nih.gov/pubmed/19170537

Wawro, B., Greenfield, N.J., Wear, M.A., Cooper, J.A., Higgs, H.N., and Hitchcock-DeGregori, S.E., 2007.
Tropomyosin regulates elongation by forming at the fast-growing end of the actin filament. Biochemistry 46(27), 8146-55. http://www.ncbi.nlm.nih.gov/pubmed/17569543

Greenfield, N.J., Huang, Y.J., Swapna, G.V., Bhattacharya, AS., Rapp, B., Singh, A., Montelione, G.V., and
Hitchcock-DeGregori, S.E. 2006. Solution NMR structure of the junction between tropomyosin molecules:
implications for actin binding and regulation. J. Mol. Biol. 364, 80-96. http://www.ncbi.nlm.nih.gov/pubmed/16999976

Singh, A., and Hitchcock-DeGregori, S.E. 2006. Dual requirement for flexibility and specificity for binding of
the coiled-coil tropomyosin to its target, actin. Structure 14, 43-50.
http://www.ncbi.nlm.nih.gov/pubmed/16407064