Education

B.S., National Taiwan University, Taiwan, Republic of China, Biochemistry, 1966

Ph.D., University of California at San Diego, La Jolla, CA, Biochemistry, 1970

Research Interests

Myosin in smooth muscle not only is the motor but also plays a role in the regulation. Phosphorylation of the regulatory light chain of myosin is required to initiate the force generation in smooth muscle contraction. It is intriguing that the function of a large molecule such as myosin consisting of a pair of heavy and two pairs of light chains with a mass of 500 kDa is controlled by a small phosphate group. Currently the major focus of my research is to correlate the structural features of smooth muscle myosin from chicken gizzard with its functions. In particular, our goal is to answer the question of how the effects of the phosphorylation of the light chains are communicated to the regions in the heavy chains that are responsible for muscle contraction?

Our strategy is to map out the communication pathway in a systematic fashion, by determining the effects of phosphorylation on the structure of light chains, the light chain- heavy chain interactions, and the actin-myosin interactions. Fluorescent or crosslinking probes will be attached to cysteine residues that have been genetically placed at strategically important positions on light chains or/and heavy chains. A number of methods such as crosslinking by disulfide formation or bifunctional reagents, fluorescence and CD measurements, resonance energy transfer technique, susceptibility to proteolysis, etc. will be used to monitor the structural changes induced by phosphorylation.

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Selected Publications

Liu, R., Leavis, P.C. & J.A. Badwey (1996) In vitro activation of a 60-70 kDa protein kinase from neutrophils by limited proteolysis. Biochim. Biophys. Acta. 1295, 89-95.

Wu, G-M, Wong, A., Fang, Q. & R. C. Lu (1998) Phosphorylation Changes the Spatial Relationship Between Glu124-Arg143 and Cys18/Cys165 of the Regulatory Light Chain in Smooth Muscle Myosin. Biochemistry, 37, 7676-7685 .

Wang, C.-L., Wang, L.-W, Xu, S., Lu, R.C., Saavedra-Alanis, V. & Bryan, J. (1991) Localization of the Calmodulin- and Actin-binding Sites of Caldesmon J. Biol. Chem. 266, 9166-9172.

Lu, R.C. & Wong, A. (1989) Glu-88 Is Close to SH-1 in the Tertiary Structure of Myosin Subfragment-1. Biochemistry 28, 4826-4829

Sutoh, K. & Lu, R.C. (1987) Identification of Two Segments, Separated by 45 kDa, of the Myosin Subfragment-1 Heavy Chain That Can Be Crosslinked to the SH-* Thiol. Biochemistry 26, 4511-4516.

Lu, R.C., Moo, L. & Wong, A. (1986) Both the 25 kDa and 50 kDa Domains in Myosin Subfragment-1 Are Close to the Reactive Thiols. Proc. Natl. Acad. Sci. USA 83, 6392-6396.

Lu, R.C. & Wong, A. (1985) The Amino Acid Sequence and Stability Predictions of the Hinge Region in Myosin Subfragment-2. J. Biol. Chem. 260, 3456-3461.

Lu, R.C. & Lehrer, S.S. (1984) Effects of Interchain Disulfide Crosslinks on the Trypsin Cleavage Pattern and Conformation of Myosin Subfragment-2. Biochemistry 23, 5975-5981.

Lu, R.C. & Szilagyi, L. (1981) Change of Reactivity of Lysine Residues Upon Actin Polymerization. Biochemistry 20, 5914-5919.

Lu, R.C. & Elzinga, M. (1978) The Primary Structure of Tubulin: Sequence of the Carboxyl-terminus and Seven Other Cyanogen Bromide Peptides form the a-Chain. Biochim. Biophys. Acta 537, 320-328.

Lu, R.C. & Elzinga, M. (1977) The Partial Amino Acid Sequence of Brain Actin and Its Homology with Muscle Actin. Biochemistry 16, 5801-5806.

Chen, R. & Doolittle, R.F. (1970) Isolation, Characterization and Location of a Donor-Acceptor Unit from Crosslinked Fibrin. Proc. Natl. Acad. Sci. USA 66, 472-479.