Postdoctoral Associate -- Molecular Basis of Nuclear Transport

As part of a long term collaboration between the Rout Lab and Cowburn Lab, we seek to appoint immediately a biochemistry/biophysics postdoctoral associate to characterize the mechanisms, interactions, and modelling associated with transport in the nuclear pore complex (NPC). Previous publications from this collaboration are listed below.

The project is focused on analysis and characterization of complexes of nucleoporins and transport factors, from simple binary complexes to the complete nuclear pore complex. The project will focus particularly on domains in certain nucleoporins with multiple intrinsically disordered Phe-Gly (FG) repeat motifs, and how these FG motifs mediate selective nucleocytoplasmic transport across the NPC through specific interactions with nuclear transport factors, which carry their cognate macromolecular cargoes. Resources include the protein expression and cell fractionation methodologies associated with the National Center for Dynamic Interactome Research , NMR resources at Rockefeller, Einstein, and NYSBC, and collaboration with the integrative modelling approaches of the Sali lab. The position will be in the Laboratory of Cellular and Structural Biology, which has an internationally recognized focus on the application of a variety of approaches towards an integrated understanding of the structure and function of the NPC.

Michael P. Rout, and David Cowburn

Interested applicants should send in a single pdf -- a cover letter, CV, and names and contact information of three (3) references to hattonb@mail.rockefeller.edu.

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1. Sparks, S.; Temel, D. B.; Rout, M. P.; Cowburn, D., Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering. Structure 2018, 26 (3), 477-484 e4.
2. Hayama, R.; Sparks, S.; Hecht, L. M.; Dutta, K.; Karp, J. M.; Cabana, C. M.; Rout, M. P.; Cowburn, D., Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex. J Biol Chem 2018, 293 (12), 4555-4563.
3. Upla, P.; Kim, S. J.; Sampathkumar, P.; Dutta, K.; Cahill, S. M.; Chemmama, I. E.; Williams, R.; Bonanno, J. B.; Rice, W. J.; Stokes, D. L.; Cowburn, D.; Almo, S. C.; Sali, A.; Rout, M. P.; Fernandez-Martinez, J., Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 2017, 25 (3), 434-445.
4. Raveh, B.; Karp, J. M.; Sparks, S.; Dutta, K.; Rout, M. P.; Sali, A.; Cowburn, D., Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex. Proc Natl Acad Sci U S A 2016, 113 (18), E2489-97.
5. Hough, L. E.; Dutta, K.; Sparks, S.; Temel, D. B.; Kamal, A.; Tetenbaum-Novatt, J.; Rout, M. P.; Cowburn, D., The molecular mechanism of nuclear transport revealed by atomic-scale measurements. Elife 2015, 4.