BBS Faculty Member - Samara Reck-Peterson

Samara Reck-Peterson

Department of Cell Biology

Harvard Medical School
LHRRB Bldg., Rm. 301C
240 Longwood Ave.
Boston, MA 02115
Tel: 617-432-7178
Fax: 617-432-7193
Email: reck-peterson@hms.harvard.edu
Lab Members: 5 postdoctoral fellows, 3 graduate students, 1 lab manager
Visit my lab page here.



The Reck-Peterson lab is broadly interested in the regulated movements of intracellular components, which allow cells to move, divide, communicate with neighboring cells, and maintain cellular homeostasis. Most eukaryotic cells are too large to rely on diffusion for these movements. Cells use molecular motors to transport intracellular components quickly in a manner that can be regulated in time and space.

Intracellular transport occurs along actin and microtubule tracks and is driven by myosins (actin-based motors) and dyneins and kinesins (microtubule-based motors). We focus on microtubule-based intracellular transport. Microtubules, which are larger and more rigid than actin filaments, are typically used for long distance, directed transport.

All eukaryotic cells use motors for transport. In humans, longer cells, such as neurons, are more sensitive to defects in transport. For example, neurodegenerative and neurodevelopmental diseases are known to result from defects in microtubule-based transport.

We use a wide variety of experimental techniques (genetics, genomics, single molecule biophysics, biochemistry, and structural biology) and intellectual frameworks (cell biology, systems biology, synthetic biology, and biophysics) to understand the molecular basis of intracellular transport.

 


Single cargo (yellow) driven by dynein motors can be seen on microtubules (blue). A kymograph (bottom) reveals extensive dynein-drive motility of cargo along microtubules.



Last Update: 1/13/2014



Publications

For a complete listing of publications click here.

 


 

Derr ND*, Goodman BS*, Jungmann R, Leschziner AE, Shih WM, Reck-Peterson SL. (2012) Tug of war in motor protein ensembles revealed with a programmable DNA origmai scaffold. Science 338: 662-665.
[Commentary on this research appeared in:
Science 338: 626-627.]

Huang J*, Robert A*, Leschziner L,
Reck-Peterson SL. (2012) Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor. Cell 150: 975-986.
[Commentary on this research appeared in:
Cell 150: 877-879.]

Redwine WB*, Hernarndez-Lopez R*, Zou S, Huang J,
Reck-Peterson SL, Leschziner AE. (2012) Structural basis for microtubule binding and release by dynein. Science 337: 1532-1536.

Egan M, Tan K, Reck-Peterson SL. (2012) Lis1 is an initiation factor for dynein-driven organelle transport.
J Cell Biol. 197: 971-982.
[Commentary on this research appeared in:
J. Cell Biol. 197: 852.]

Qiu W*, Derr ND*, Goodman BS, Villa E, Wu D, Shih W,
Reck-Peterson SL. (2012) Dynein achieves processive motion using both stochastic and coordinated stepping. Nat Struct Mol Biol 19: 193.
[Commentary on this research appeared in:
Nature 482: 7383.]

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.
[Commentaries on this research appeared in: Cell, 126: 335-348,
Nat. Rev. Mol. Cell Biol. 7: 625, and J. Cell Biol. 172: 486-92].



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