[3dem] postdoctoral position available at UC San Diego
aleschziner at ucsd.edu
Sun Sep 10 14:50:06 PDT 2017
Postdoctoral position to study dynein structure and mechanism available at UC San Diego
A postdoctoral position is available in the labs of Samara Reck-Peterson and Andres Leschziner at UC San Diego. The two groups have a long-standing collaboration to study the mechanism and regulation of cytoplasmic dynein using a combination of biochemistry, single-molecule biophysics, cryo-electron microscopy (cryo-EM) and cell biology (1-6).
The two laboratories are fully equipped for all aspects of biochemistry, cell biology, single-molecule biophysics and cryo-EM. Dr. Reck-Peterson is the faculty director of the newly-formed Nikon Imaging Center at UC San Diego, which will house five state-of-the-art light microscopes. In addition, the Reck-Peterson lab is equipped with two total internal reflection microscopes for single-molecule imaging and recently built a lattice light sheet microscope for live-cell imaging. The Leschziner lab is a core member of the UC San Diego Cryo-EM Facility, which houses their own FEI Talos Arctica equipped with a K2 Summit, an FEI Polara, an FEI Titan Krios (to be installed in December), which will be equipped with a K2 Summit and a Quantum energy filter. The Facility also has a cryo-capable Tecnai Sphera used for general screening.
Candidates must have a Ph.D. at the start of the postdoctoral appointment. Research experience in the following area(s) is particularly desirable: (1) cryo-EM and/or (2) biochemistry of large protein complexes.
Potential candidates should send a PDF including cover letter, curriculum vitae with list of publications, and names of three referees to:
Professor Samara Reck-Peterson - email: sreckpeterson at ucsd.edu<mailto:sreckpeterson at ucsd.edu>
Professor Andres Leschziner - email: aleschziner at ucsd.edu<mailto:aleschziner at ucsd.edu>
Applications will be reviewed as they are received and until the position is filled. UC San Diego is an equal opportunity employer committed to diversity.
1. DeSantis ME#, Cianfrocco MA#, Htet ZM#, Tran PT, Reck-Peterson SL* and Leschziner AE* (2017) Lis1 has two opposing modes of regulating cytoplasmic dynein Cell 170: 1197-1208.
2. Cianfrocco MA#, DeSantis ME#, Leschziner AE and Reck-Peterson SL (2015). Mechanism and regulation of cytoplasmic dynein. Annu. Rev. Cell Dev. Biol. 31: 83-108.
3. Toropova K#, Zou S#, Roberts AJ, Redwine WB, Goodman BS, Reck-Peterson SL* and Leschziner AE* (2014). Lis1 regulates dynein by sterically blocking its mechanochemical cycle. eLife 3:e03372
4. Derr N#, Goodman BS#, Jungmann R, Leschziner AE, Shih W and Reck-Peterson SL (2012). Tug of war in motor protein ensembles revealed with a programmable DNA origami scaffold. Science 338: 662.
5. Redwine WB#, Hernandez-Lopez RH#, Zou S, Huang J, Reck-Peterson SL and Leschziner AE (2012). Structural basis for microtubule binding and release by dynein. Science 337: 1532
6. Huang J#, Roberts AJ#, Leschziner AE and Reck-Peterson SL (2012). Lis1 acts as a “clutch” between the ATPase and and microtubule-binding domains of the dynein motor. Cell 150(5): 975
# equal contribution
* co-corresponding authors
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