Janice L. Robertson, Ph.D.

Assistant Professor
Biochemistry and Molecular Biophysics

Biochemistry, Biophysics, and Structural Biology Program
Computational and Systems Biology Program
Neurosciences Program

  • 314-273-7758

  • 314-273-1682

  • MCD 223

  • janice.robertson@wustl.edu

  • https://www.robertsonlaboratory.com

  • membrane protein; single-molecule; TIRF microscopy; protein folding; thermodynamics; lipids; oligomerization

  • To understand how and why membrane proteins fold, form stable complexes, and achieve conformational stability inside of the oil-filled cell membrane.

Research Abstract:

Throughout my training, I have built a foundation of experience enabling my laboratory to investigate important biological questions by integrating theory and experimental approaches hand in hand. For my undergraduate education. I obtained a Honours Bachelor of Science degree at the University of Toronto in Theoretical Physiology and Mathematics which taught me how to model biological systems using principles of math, physics and chemistry. I was first introduced to membrane proteins in the laboratory of Dr. Peter Backx, where I carried out research on the mathematical modeling of the cardiac action potential as well as experimental. electrophysiological studies of voltage-gated sodium channels. During my PhD with Dr. BenoTt Roux and Dr. Larry Palmer at the Weill Cornell Graduate School of Medical Sciences, I applied these fundamentals to computational studies aimed at investigating how changes in inward rectifier potassium channel sequence leads to changes in function (Robertson and Roux, 2005; Zhang et al., 2004; Robertson et al., 2008; 2012; 2010b). My postdoctoral training with Dr. Chris Miller at HHMI/Brandeis University immersed me in experimental membrane protein biochemistry, investigating the structure and function of anion transporters and channels (Jayaram et al., 2011; Robertson et al., 2010a; Stockbridge et al., 2013). After receiving a K99 award, I studied with Dr. Jeff Gelles at Brandeis University to learn single-molecule fluorescence microscopy and apply this technique to the study of reversible CLC dimerization in lipid bilayers as a model system to investigate the physical driving forces involved in self-assembly of proteins in membranes.

The subject of membrane protein biochemistry is currently primed for a productive combination of theory and experiments. With my background, I am uniquely trained to integrate these areas into one laboratory and overcome the hurdles currently existing in the field while training the next generation of interdisciplinary scientists. In July 2013, I set up my laboratory at the University of Iowa in the Department of Molecular Physiology and Biophysics, and in September 2018, we moved to the Department of Biochemistry and Molecular Biophysics at Washington University. In my lab, we integrate experimental techniques such as biochemistry, electrophysiology, crystallography and single-molecule Total Internal Reflection Fluorescence (TIRFJ microscopy, with theoretical computer modeling, to study membrane protein systems in membranes. We have built our own multi-color co-localization TIRF microscope (Lambda II, and now Ill) following the Gelles lab design, which has fostered numerous collaborations with membrane protein physiologists interested in single-molecule and whole-cell TIRF imaging (e.g. Ahern laboratory, University of Iowa (Leisle et al., 2016); Sah Laboratory, University of Iowa and Washington University, ROl DK106009, NIH/NIDDK; Senes Laboratory CHE-1710183, NSF. University of Wisconsin - Madison).

However, the primary goal of my laboratory is to understand how and why membrane proteins self-assemble (i.e. fold), form stable complexes. and achieve conformational stability inside of the oil-filled cell membrane. This is a challenging, and consequently, poorly understood area that is fundamental to cell biology.

Selected Publications:

Robertson JL (2018). The lipid bilayer membrane and its protein constituents. Journal of General Physiology 150 ( 11). doi: 10.0185/jgp.201812153

Chadda R, Cliff L, Brimberry M & Robertson JL (2018). A model-free method for measuring dimerization free energies of CLC-ecl in lipid bilayers. Journal of General Physiology. 2018 Jan 10, doi: 10.1085/jgp.201711893, PMID: 29321261
(biorXiv 154286; doi:10.1101 /154286). Commentary by KF Fleming, "Taking deterministic control of membrane protein monomer-dimer measurements" J. Gen Physiol. 2018 Jan 17, pii: jgp.201711913. doi: 10.1085/jgp201711913.

Condon SGF+.Mahbuba DA+, Armstrong CR, Dias-Vazquez G, Craven SJ, LaPointe LM, Khadria AS, Chadda R, Crooks JA. Rangarajan N, Weibel DB, Hoskins AA, Robertson JL, Cui Q & Senes A (2017). The FtsLB sub-complex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions. J Biol Chem. 2017 Dec 12, doi: 10.1074/jbc.RA 117.000426 +shared first authorship

Leisle L, Chadda R, Lueck JD, Infield DT, Galpin JD, Krishnamani V, Robertson JL & Ahern CA (2016). Cellular encoding of Cy dyes for single-molecule imaging. eLife 2016; 10.7554/eLife.19088.

Last Updated: 2/22/2019 1:07:58 PM

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