Open Postdoctoral position, faculty mentor Tino Pleiner

Postdoctoral Fellow Position: Ion Channel Biogenesis and Quality Control

Summary: The Pleiner Lab at Stanford University is seeking a highly motivated postdoctoral fellow to investigate the molecular mechanisms that govern ion channel folding, assembly, and quality control at the human endoplasmic reticulum (ER) membrane. The project will combine cutting-edge approaches in functional genomics, mechanistic cell biology, cryo-electron microscopy, and protein engineering. We are particularly interested in candidates that can combine mechanistic cell biology with functional genomics and/or structural biology.

Lab and project background: Neuronal and cardiac ion channels are essential mediators of action potentials, enabling neuronal signal transmission and coordinated heart muscle contraction. Precise electrical signaling depends on the correct identity, abundance, localization, and relative balance of multiple ion channels. Consequently, mutations that disrupt ion channel biogenesis or delivery to the plasma membrane can have profound consequences for human health, contributing to cardiac arrhythmias, movement disorders, and neurological conditions such as epilepsy—diseases that collectively affect millions of people worldwide. Our lab is broadly interested in understanding how excitable cells produce diverse ion channels with the appropriate quality, quantity, and stoichiometry to support proper membrane electrical activity. In this project, the successful candidate will work with a collaborative and supportive team of biochemists, cell biologists, and structural biologists to uncover the molecular machinery and mechanisms that regulate ion channel membrane insertion, assembly, and quality control at the ER.

This position offers substantial opportunities for scientific independence and creativity. The successful candidate will help shape the direction of the project, develop and apply innovative experimental approaches, and have opportunities to mentor graduate and undergraduate students.

Environment: The Pleiner Lab is an inclusive, collegial environment that values curiosity, learning, teamwork, and mentorship. As a member of a small and growing lab, the successful candidate will benefit from close mentorship by the principal investigator, outstanding resources, and access to Stanford’s exceptional collaborative research environment. In particular, the Department of Molecular and Cellular Physiology provides an ideal setting for this work, bringing together world-leading researchers who investigate fundamental cellular mechanisms, with a strong emphasis on the structure and function of disease-relevant membrane proteins. Stanford also offers world-class core facilities and a rich professional-development environment, including structured mentoring programs, workshops and training opportunities, seminar series, and annual departmental retreats. Beyond the lab, the sunny Northern California Bay Area offers exceptional culinary, cultural, and outdoor recreational opportunities.

Relevant publications:

Stanton, M.*, Singal, B.*, Biswal, M. N.*, Agarwal, M.*, Scheuing, C. E., Vargas, G. D., Gao, A., Gifford, C. A. and Pleiner, T., The ER membrane protein complex acts as a chaperone to promote the biogenesis of multi-bundle membrane proteins. bioRxiv https://doi.org/10.64898/2026.01.14.699575 (2026).

Stevens, T.A., Tomaleri, G.P., Hazu, M., Wei, S., Nguyen, V.N., DeKalb, C., Voorhees, R.M.† and Pleiner, T.† (2024) A nanobody-based strategy for rapid and scalable purification of native human protein complexes. Nature Protocols 19, 127–158. 

Pleiner, T.*, Hazu, M.*, Tomaleri, G.P.*, Nguyen, V.N., Januszyk, K. and Voorhees, R.M. (2023) A selectivity filter in the EMC limits protein mislocalization to the ER. J Cell Biol, 222, e202212007.

Pleiner, T., Hazu, M., Tomaleri, G.P., Januszyk, K., Oania, R.S., Sweredoski, M.J., Moradian, A., Guna, A. and Voorhees, R.M. (2021) WNK1 is an assembly factor for the human ER membrane protein complex. Mol Cell, 81, 2693-2704.e12.

Pleiner, T.*, Tomaleri, G.P.*, Januszyk, K.*, Inglis, A.J., Hazu, M. and Voorhees, R.M. (2020) Structural basis for membrane insertion by the human ER membrane protein complex. Science, 369, 433-436.