|
Faculty
Stephen M. King
Professor of Biochemistry
Associate Director, Graduate Program in Molecular Biology and
Biochemistry
sking@nso2.uchc.edu
Dyneins are microtubule-based molecular motors that power both
ciliary/flagellar motility and a variety of essential intracellular
motile events. In order for these massive enzymes to function correctly,
they must be attached to the appropriate cargo and motor activity must
be precisely regulated. Over the last few years we have identified a
series of highly intriguing dynein components that appear to be involved
in these regulatory activities. Current focus in the laboratory is on
understanding the mechanisms which control motor function using a wide
variety of techniques ranging from physiological measurements and
genetic analyses to structural biology.
Laboratory
Page
Selected Publications:
Wu, H., Blackledge, M., Maciejewski, M.W., Mullen, G.P. & King, S.M.
(2003) Relaxation-based structure refinement and backbone molecular
dynamics of the dynein motor domain-associated light chain.
Biochemistry in press.
Harrison, A., Sakato, M., Tedford, H.W., Benashski, S.E., Patel-King,
R.S. & King, S.M. (2002) Redox-based control of the g heavy chain ATPase
from Chlamydomonas outer arm dynein. Cell Motility and the
Cytoskeleton 52, 131-143.
Patel-King, R.S., Benashski, S.E. & King, S.M. (2002) A bipartite
Ca2+-regulated nucleoside diphosphate system within the Chlamydomonas
flagellum. The regulatory subunit p72. Journal of Biological
Chemistry 277, 34271-34279.
King, S.M. (2002) Dynein motors: structure, mechanochemistry and
regulation. “Molecular Motors” (Schliwa, M.; Editor), Wiley-VCH,
in press.
DiBella, L.M. & King, S.M. (2001) Dynein motors of the Chlamydomonas
flagellum. International Review of Cytology 210, 227-268.
Wu, H.W., Maciejewski, M.W., Marintchev, A., Benashski, S.E., Mullen,
G.P. & King, S.M. (2000) Solution structure of a dynein motor
domain-associated light chain. Nature Structural Biology 7,
575-579. |
