Sarah Rice, PhD
Research clusters: Cellular and Molecular Biology
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Active transport one of the hallmark processes defining life. Within eukaryotic cells, active transport of cargoes is driven by a surprisingly small set of molecular motor proteins. There are three broad classes of these motor proteins: kinesins, which generally move toward the plus ends of microtubules, dyneins, which move toward microtubule minus ends, and myosins, which move along actin filaments.
Our research is centered around the question of how kinesin motors know what cargo to pick up, when, and where to take it within cells.
A single type of kinesin motor can perform many different jobs, transporting distinct cargoes to specific locations. Kinesins also cooperate with other motors to transport cargoes bidirectionally along microtubules and to link the microtubule, actin, and intermediate filament cytoskeletons. The cell can initiate or stop kinesin-driven movement of specific cargoes in response to several types of regulatory cues. We have studied several kinesin regulators, including inhibitory domains within the kinesin motor itself, separate regulator proteins acting on kinesin motors, and post-translational modifications. By gaining a detailed biochemical and biophysical understanding of these regulatory mechanisms, we aim to understand and to be able to manipulate kinesin-driven cargo movement at the molecular level.
The regulatory machinery governing kinesin motor activity is critical to human health. Mis-regulation of kinesin motors or mis-localization of cargoes has been implicated in diseases such as Parkinson’s disease and neurofibromatosis. In addition, drug inhibitors of kinesin motors have been proposed and tested as potential anti-cancer therapeutics. Our work may lead to improvements in the development of improved drug interventions for diseases implicating kinesins.
Dietrich, K.A., Sindelar, C.V., Brewer, P., Cremo, C.R., Downing, K.H., and Rice, S.E. (2008). “The kinesin-1 motor protein is regulated by a direct interaction of its head and tail.” PNAS 105(26):8938-8943.
McMahon, P.M., Hostetter, D.R., and Rice, S.E. (2008). Temperature dependence of Dictyostelium and nonmuscle myosin-IIA tail fragment assembly. Journal of Muscle Research and Cell Motility 29(2-5):109-18
Wong, Y.L., Dietrich, K.A., Naber, N., Cooke, R., and Rice, S.E. (2009). The kinesin-1 tail conformationally restricts the nucleotide pocket. Biophysical Journal 96(7):2799-807
Larson, A.G., Landahl, E.C., and Rice, S.E. (2009). Mechanism of cooperative behavior in systems of slow and fast molecular motors. Physical Chemistry Chemical Physics 11(24):4890-8
Ally, S., Larson A.G., Barlan, K., Rice S.E., Gelfand VI. (2009). Opposite-polarity motors activate one another to trigger cargo transport in live cells. J Cell Biol. 187(7):1071-82.
Seeger, M.A. and Rice, S.E. (2010). Microtubule-associated protein-like binding of the kinesin-1 tail to microtubules. Journal of Biological Chemistry 285(11):8155-62.
Bensenor, L.B., Barlan, K., Rice, S.E., Fehon, R.G., Gelfand, V.I. (2010). Microtubule-mediated transport of the tumor suppressor Merlin. PNAS 107(16):7311-16.
Larson, A.G., Naber, N., Pate, E.F., Cooke, A.R., and Rice, S.E. (2010). The conserved L5 loop is a nucleotide exchange factor for kinesin-5 motors. Biophysical Journal 98(11):2619-27.
Wong, Y.L. and Rice, S.E. (2010). Kinesin’s light chains inhibit the head- and microtubule-binding activity of its tail. PNAS 107(26):11781-6
Landahl, E. C., Antipova, O., Bongaarts, A., Barrea, R., Berry, R.W., Binder, L.I., Irving, T., Orgel, J., Vana, L. and Rice, S.E. (2011). X-ray diffraction from intact tau aggregates in human brain tissue. Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment 649:184-187.
Naber, N., Larson, A.G., Rice, S.E., Cooke, R. Pate, E.F. (2011). Multiple conformations of the nucleotide site of kinesin-family motors in the triphosphate state. Journal of Molecular Biology 408(4):628-42.
Wang, X., Winter, D., Ashrafi, G., Schlehe, J, Wong, Y.L., Selkoe, D., Steen, J., LaVoie, M., Rice, S.E., and Schwarz, T. (2011). PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility. Cell, 147(4):893-906.
Waitzman, J.S., Larson, A.G., Cochran, J., Naber, N., Cooke, R., Pate, E.F., and Rice, S.E. (2011). The neck-linker is the primary means of head-head communication in the Eg5 dimer. Biophysical Journal 101(11):2760-9.
Seeger, M.A., Zhang, Y., and Rice, S.E. (2012). Kinesin Tail Domains Are Intrinsically Disordered. In Press, Proteins: Structure, Function, and Bioinformatics. Available online 7/7/12.
View Publications by Sarah Rice listed in the National Library of Medicine (PubMed).
DGP Faculty (Chicago Campus)
- Alphabetical List of DGP Faculty
- Cancer Biology
- Cell Biology
- Chemical Biology and Drug Discovery
- Developmental Biology
- Evolutionary Biology
- Genetics, Genomics and Molecular Biology
- Immunology and Microbial Pathogenesis
- Signal Transduction
- Structural Biology and Biochemistry
- Biomedical Informatics