We are investigating the mechanisms by which molecules are spatially organized within living cells. A main focus is on dynein, a large but poorly understood motor protein that uses ATP hydrolysis to transport cellular components and signals along microtubules. The overarching goal of our research is to understand how dynein works as a force-generating machine, and how dynein molecules are regulated to bring about coherent cellular functions. An additional interest is how defects in the dynein machinery cause human neurological disorders. Core techniques in our research are molecular electron microscopy, protein engineering, and single-molecule fluorescence microscopy.

Roberts AJ*, Goodman BS, Reck-Peterson SL*. (2014) Reconstitution of dynein transport to the microtubule plus end by kinesin. eLIFE. 3:e02641 Huang J*, Roberts AJ*, Leschziner AE, Reck-Peterson SL. (2012) Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor. Cell 150(5):975-86. Roberts AJ, Numata N, Walker ML, Kato YS, Malkova B, Kon T, Ohkura R, Arisaka F, Knight PJ, Sutoh K, Burgess SA. (2009) AAA+ Ring and linker swing mechanism in the dynein motor. Cell 136(3):485-95. Roberts AJ*, Kon T, Knight PJ, Sutoh K, Burgess SA*. (2013) Functions and mechanics of dynein motor proteins. Nature Reviews Molecular Cell Biology. 14:713-726.