Daniel P. Kiehart

Professor of Biology

Office: 
4330 French Family Science Center, Science Drive, Duke University, Durham, NC 27708-0338
Campus Box: 
Box 90338, Dept. Biology, Duke University, Durham, NC 27708-1000
Phone: 
(919) 613-8157
Our intellectual focus is on identifying determinants of cell shape that function during development. Utilizing molecular genetic and reverse genetic approaches in Drosophila, we have shown that conventional nonmuscle myosin is necessary for driving both cell division and post-mitotic cell shape changes for morphogenesis, and cellular locomotions. Currently, we are investigating how myosin elicits cell shape change and how its function is regulated through filament formation, phosphorylation, sub-cellular targeting and small GTP-binding protein function. We are characterizing myosin light chain kinase; a novel myosin VII heavy chain; and additional elements that participate in localizing myosin and transmitting the forces that it produces. We used screens for aberrant cell shape induced in the yeast S. pombe by expression of transfected Drosophila cDNAs. These experiments show that elements that define cell shape are conserved throughout phylogeny and that a screen in yeast is a valuable tool for recovering heterologous cDNAs that encode cytoskeletal elements and the proteins that regulate them. In fly, we are identifying gene products that are necessary for myosin function by genetically recovering second site non-complementing loci and biochemically recovering proteins that bind to myosin. To date, our experiments identify ~30 loci that genetically interact with myosin and a kinase activity that phosphorylates myosin heavy chain and establish genetically, that the Rho signalling pathway is required in concert with nonmuscle myosin II for morphogenesis. We are also using manipulation studies to understand the forces that drive cellularization and morphogenesis. We show that both the amnioserosa and the leading edge of the lateral epidermis contribute to the movements of dorsal closure. Finally, we are examining the role these proteins play in movements that occur during wound healing.

Education

  • Ph.D., University of Pennsylvania 1979

  • B.A., University of Pennsylvania 1973

Kiehart, DP. "The actin membrane skeleton in Drosophila development." Semin Cell Biol 1, no. 5 (October 1990): 325-339. (Review)

Ketchum, AS, Stewart, CT, Stewart, M, and Kiehart, DP. "Complete sequence of the Drosophila nonmuscle myosin heavy-chain transcript: conserved sequences in the myosin tail and differential splicing in the 5' untranslated sequence." Proc Natl Acad Sci U S A 87, no. 16 (August 1990): 6316-6320.

Kiehart, DP. "Molecular genetic dissection of myosin heavy chain function." Cell 60, no. 3 (February 9, 1990): 347-350. (Review)

Kiehart, DP, Ketchum, A, Young, P, Lutz, D, Alfenito, MR, Chang, XJ, Awobuluyi, M, Pesacreta, TC, Inoué, S, and Stewart, CT. "Contractile proteins in Drosophila development." Ann N Y Acad Sci 582 (1990): 233-251. (Review)

Dubreuil, RR, Byers, TJ, Stewart, CT, and Kiehart, DP. "A β-spectrin isoform from Drosophila (βH) is similar in size to vertebrate dystrophin." Journal of Cell Biology 111, no. 5 (1990): 1849-1858.

Pesacreta, TC, Byers, TJ, Dubreuil, R, Kiehart, DP, and Branton, D. "Drosophila spectrin: the membrane skeleton during embryogenesis." J Cell Biol 108, no. 5 (May 1989): 1697-1709.

Kiehart, DP, Lutz, MS, Chan, D, Ketchum, AS, Laymon, RA, Nguyen, B, and Goldstein, LS. "Identification of the gene for fly non-muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family." EMBO J 8, no. 3 (March 1989): 913-922.

Dubreuil, R, Byers, TJ, Branton, D, Goldstein, LS, and Kiehart, DP. "Drosophilia spectrin. I. Characterization of the purified protein." J Cell Biol 105, no. 5 (November 1987): 2095-2102.

Byers, TJ, Dubreuil, R, Branton, D, Kiehart, DP, and Goldstein, LS. "Drosophila spectrin. II. Conserved features of the alpha-subunit are revealed by analysis of cDNA clones and fusion proteins." J Cell Biol 105, no. 5 (November 1987): 2103-2110.

Pages