Samara Reck-Peterson

Department of Cell Biology
Harvard Medical School
Seeley G. Mudd Building, Room 529
240 Longwood Avenue, Boston, MA 02115

tel: (617) 432-7178; fax: (617) 432-7193
email: reck-peterson@hms.harvard.edu
web: http://reck-peterson.med.harvard.edu

Research Interests:

Single Molecule Studies of Cellular Motors
Molecular motors and the tracks they move along are responsible for generating, maintaining and remodeling internal cellular organization. Our research efforts are focused on cytoplasmic dynein, a molecular motor that moves on microtubule tracks and transports dozens of essential cargos in mammalian cells. Cytoplasmic dynein is arguably the most challenging and understudied cytoskeletal motor protein. Understanding how dynein works as a molecular machine has been challenging due to its size (>1.5 MDa) and many associated subunits. By using molecular biology and genetics techniques we have generated a biochemical source of recombinant dynein and all of its associated subunits. We use total internal reflection light microscopy to observe movements made by single dynein molecules. We are also collaborating with Andres Leschziner’s lab (Department of Molecular and Cellular Biology, FAS) to study the structure of dynein and dynein complexes by single particle cryo-electron microscopy.

Mechanism of Microtubule Transport
The microtubule cytoskeleton and the molecular motors that move along it—dynein and kinesin—are responsible for powering the movement of chromosomes during mitosis and of organelles, signaling molecules and RNAs in the cytoplasm. The spatial and temporal regulation involved in transporting these cargos at the cellular level remains one of the big unsolved questions in the field of cell biology. We are using the filamentous fungus, Aspergillus nidulans, as a model system to dissect the molecular mechanisms of microtubule-based transport. Aspergillus’ polarized hyphae, whose rapid growth requires microtubule-based transport, and its high frequency of homologous recombination make it an ideal model organism for studying transport. We are currently designing fungal strains that will be used to perform high-throughput microscopy-based screens to identify novel molecules required for dynein- or kinesin-based motility. Ultimately, we aim to reconstitute motor-cargo transport in vitro and to develop methods to observe the dynamics of transport in vivo with nanometer precision.

 

Selected Publications:

Cho, C., Reck-Peterson, S.L., Vale, R.D. (2008). Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation. J. Biol. Chem. 283(38): 25839-45.

Gennerich A., Carter A.P., Reck-Peterson, S.L., and Vale, R.D. (2007). Force-Induced Bidirectional Stepping of Cytoplasmic Dynein. Cell 131: 952-65.

Reck-Peterson, S.L., Yildiz, Y., Carter, A.P., Gennerich, A., Zhang, N., and Vale, R.D. (2006). Single molecule analysis of dynein processivity and stepping behavior. Cell 126: 335-348.

Gibbons, I.R., Garbarino, J.E., Tan, C.E., Reck-Peterson, S.L., Vale, R.D., Carter, A.P. (2005). The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk. J. Biol. Chem. 280(25): 23960-5.

 

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