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Stephen M. King

Professor of Biochemistry
Director, Graduate Program in Molecular Biology and Biochemistry
sking@nso2.uchc.edu

Stephen M. King
Areas of Interest

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.

Lab Rotation Projects

1) Examination of dynein components as candidates for high resolution structural analysis.

2) Genetic screen for mutants defective in flagellar motility.

3) Biochemical approaches to defining intra-dynein associations.

4) Functional analysis of dyneins expressing mutant components.

5) Function of flagellar-associated nucleoside diphosphate kinases.

6) Chlamydomonas metabolomics using NMR and/or mass spectrometry.

Selected Publications

Wanschers B, van de Vorstenbosch R, Wijers M, Wieringa B, King SM, Fransen J. Rab6 family proteins interact with the dynein light chain protein DYNLRB1. Cell Motil Cytoskeleton. 2008 Mar;65(3):183-96.

Lo KW, Kogoy JM, Rasoul BA, King SM, Pfister KK. Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate chains reveals novel intersubunit regulation during assembly of the dynein complex. J Biol Chem. 2007 Dec 21;282(51):36871-8. Epub 2007 Oct 27.

Wakabayashi K, Sakato M, King SM. Protein modification to probe intradynein interactions and in vivo redox state. Methods Mol Biol. 2007;392:71-83.

Rompolas P, Pedersen LB, Patel-King RS, King SM. Chlamydomonas FAP133 is a dynein intermediate chain associated with the retrograde intraflagellar transport motor. J Cell Sci. 2007 Oct 15;120(Pt 20):3653-65.

Sakato M, Sakakibara H, King SM. Chlamydomonas outer arm dynein alters conformation in response to Ca2+. Mol Biol Cell. 2007 Sep;18(9):3620-34.

Pedersen LB, Rompolas P, Christensen ST, Rosenbaum JL, King SM.
The lissencephaly protein Lis1 is present in motile mammalian cilia and requires outer arm dynein for targeting to Chlamydomonas flagella.
J Cell Sci. 2007 Mar 1;120(Pt 5):858-67.

Hozumi A, Satouh Y, Makino Y, Toda T, Ide H, Ogawa K, King SM, Inaba K.
Molecular characterization of Ciona sperm outer arm dynein reveals multiple components related to outer arm docking complex protein 2.
Cell Motil Cytoskeleton. 2006 Oct;63(10):591-603.

Wakabayashi K, King SM. Modulation of Chlamydomonas reinhardtii flagellar motility by redox poise. J Cell Biol. 2006 Jun 5;173(5):743-54.

Yang P, Diener DR, Yang C, Kohno T, Pazour GJ, Dienes JM, Agrin NS, King SM, Sale WS, Kamiya R, Rosenbaum JL, Witman GB. Radial spoke proteins of Chlamydomonas flagella. J Cell Sci. 2006 Mar 15;119(Pt 6):1165-74.

Pfister KK, Shah PR, Hummerich H, Russ A, Cotton J, Annuar AA, King SM, Fisher EM. Genetic analysis of the cytoplasmic dynein subunit families.
PLoS Genet. 2006 Jan;2(1):e1.

  
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