phone: (310) 794-2103
office: 1121 TLSB
research interests: Molecular Basis of Muscle Function and Muscular Dystrophy
The goals of my research program are to (1) investigate the interaction and regulation of macromolecular adhesion complexes at the cell surface in normal and dystrophic skeletal and cardiac muscle, (2) elucidate the mechanisms that improve muscle cell adhesion to its surrounding extracellular matrix and govern muscle growth, and (3) use these basic discoveries to develop therapeutics that prevent muscle wasting. Our lab is focused on Duchenne muscular dystrophy, which is the most common lethal disorder of children. Genetic mutations in the dystrophin gene cause Duchenne muscular dystrophy, which is an X-linked disease that affects skeletal and cardiac muscle. We have discovered that the dystrophin associated protein, sarcospan, ameliorates muscle, cardiac, and respiratory dysfunction in mouse models of Duchenne muscular dystrophy. Sarcospan increases the expression of compensatory proteins that protect the muscle myofiber from contraction-induced injury. We are currently translating these results using pharmacological and genetic approaches. We are actively engaged in the Center for Duchenne Muscular Dystrophy at UCLA and the Senator Paul D. Wellstone Center of Excellence Partnership between Northwestern University, University of Florida, and UCLA. In addition to our research program in muscular dystrophy, we are also actively engage in STEM education research that is focused on the role of teaching with technology to create inclusive learning communities.
Peter, A.P., Miller, G., Capote, J., DiFranco, M., Solares-Perez, A., Wang, E.L., Heighway, J., Coral-Vazquez, R., Vergara, J., and Crosbie-Watson, R.H., "Identification of nanospan, a new isoform of sarcospan, that localizes to the sarcoplasmic reticulum in skeletal muscle", Skeletal Muscle, in revision, (2017) .
McMorran, B.J., McCarthy, F.E., Gibbs, E.M., Pang, M., Marshall, J.L., Nairn, A.V., Moremen, K.W., Crosbie-Watson, R.H., and Baum, L.G., "Differentiation-related glycan epitopes identify discrete domains of the muscle glycocalyx", Glycobiology, 26 : 1120-1132 (2016) [link].
Gibbs, E.M., Marshall, J.L., Ma, E., Nguyen, T.M., Hong, G., Lam, J. Spencer, M.J., and Crosbie-Watson, R.H., "High levels of sarcospan are well tolerated and act as a sarcolemmal stabilizer to address skeletal muscle and pulmonary dysfunction i DMD", Hum. Mol. Genet, 25 : 5395-5406 (2016) [link].
Parvatiyar, M.S., Marshall, J.L., Nguyen, R.T., Jordan, M.C., Richardson, V.A., Roos, K.P., and Crosbie-Watson, R.H., "Sarcospan Regulates the Cardiac Hypertrophic Response and Prevents Cardiomyopathy Associated with Duchenne Muscular Dystrophy", J. Am. Heart Association, (2015) .
Marshall, J.L., Kwok, J., McMorran, B.J., Baum, L.G. and Crosbie-Watson, R.H., "The potential of sarcospan in adhesion complex replacement therapeutics for the treatment of muscular dystrophy", FEBS J, 280 : 4210-4229 (2013) [link].
Marshall, J.L. and Crosbie-Watson, R.H., "Sarcospan: a small protein with big potential for Duchenne muscular dystrophy", Skeletal Muscle, 3 (1): (2013) [link].
Rutkowshi, A., Bonneman, C., Brown, S., Thorsteinsdottir, S., Dominov, J., Ruegg, M.A., Matter, M., Guttridge, D., Crosbie-Watson, R.H., Kardon, G., Nagaraju, K., Girgenrath, M. and Burkin, D.J., "Report on the Myomatrix conference", Neuromuscl. Disord, 1-4 (2012) [link].
Marshall, J.L. and Crosbie-Watson, R.H., "Sarcospan: a small protein with large potential for Duchenne muscular dystrophy", Skeletal Muscle, (2012) .
Marshall, J.L., Chou, E., Oh, J., Kwok, A., Burkin, D.J. and Crosbie-Watson, R.H., "Dystrophin and utrophin expression requires sarcospan: loss of alpha 7 integrin exacerbates a newly discovered muscle phenotype in sarcospan-null mice", Hum. Mol. Genet, 21 : 4378-4393 (2012) [link].
Cabrera, P.V., Pang, M., Marshall, J.L., Kung, R., Nelson, S.F., Stalnaker, S.H., Wells, L., Crosbie-Watson, R.H. and Baum, L.G., "High-throughput screening for compounds that alter muscle cell glycosylation identifies new role for N-glycans in regulating sarcolemmal protein abundance and laminin binding", J. Biol. Chem, 287 : 22759-22770 (2012) [link].