Joanne Lemieux


Ph.D, New York University (2002)
M.Sc., Dalhousie University (1994)
Office: 780-492-3586
Lab: 780-492-3465
Fax: 780-492-0886



Membrane proteins are key targets for the drug development. Our research centers around studying membrane proteins involved in disease, using X-ray crystallography and other biophysical techniques, to reveal structural, functional and mechanistic details of membrane proteins that could one day aid in the development of new drugs and vaccines targeted towards membrane proteins.

One major focus of the lab is the study of rhomboid intramembrane proteases (peptidases). Rhomboid function has been linked to Parkinson's disease, breast cancer and parasitic invasion. Our crystal structures of this novel type of protease are providing information on how the rhomboid protease acts to cleave protein targets in the membrane. Using both functional and structural approaches we are focusing on how rhomboid proteases regulate cleavage of their substrates. This information is crucial to assist with de novo drug design.


Selected Publications:

Rhomboid intramembrane protease:

Activity Assays for Rhomboid Proteases.
Arutyunova E, Strisovsky K, Lemieux MJ.
Methods in Enzymology (2017) 584, 395-437.

Production of Recombinant Rhomboid Proteases.
Arutyunova E, Panigrahi R, Strisovsky K, Lemieux, MJ.
Methods in Enzymology (2017) 584, 255-278.

Reversible unfolding of rhomboid intramembrane proteases.
Panigrahi R, Arutyunova E, Panwar P, Gimpl K, Keller S, Lemieux MJ.
Biophys J (2016) 110(6).

Probing Catalytic Rate Enhancement During Intramembrane Proteolysis.
Arutyunova E, Smithers CC, Corradi V, Espiritu AC, Young HS, Tieleman DP, Lemieux MJ.
Biol Chem. (2016) Sep 1;397(9)

Allosteric regulation of rhomboid intramembrane proteolysis.
Arutyunova E, Panwar P, Skiba PM, Gale N, Mak MW, Lemieux MJ.
EMBO J. (2014) Sep 1;33(17):1869-81.

The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.
Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, James MN.
Proc Natl Acad Sci U S A, (2007) v. 104, p. 750-4.


Lipid biosynthetic enzymes:

Brassica napus diacylglycerol acyltransferase 1 is regulated by its hydrophilic N-terminal domain in response to allosteric effectors.
Caldo KMP, Acedo JZ, Panigrahi R, Vederas JC, Weselake RJ, Lemieux MJ.
Plant Physiol. (2017) Oct;175(2):667-680.

Different factors contribute to increased neutral lipid content in yeast producing plant DGAT1 variants.
Xu Y, Chen G, Greer MS, Caldo KMP, Ramakrishnan G, Shah S, Wu L, Lemieux MJ, Ozga J, Weselake RJ.
J Biol Chem. (2017) Sep 12. pii: jbc.M117.811489. doi: 10.1074/jbc.M117.811489.

Purification and properties of recombinant Brassica napus diacylglycerol acyltransferase 1.
Caldo KM, Greer MS, Chen G, Lemieux MJ, Weselake RJ.
FEBS letters (2015) 589(6):773-8.



Fluorescent Hexose Conjugates Establish Stringent Stereochemical Requirement by GLUT5 for Recognition and Transport of Monosaccharides.
Soueidan OM, Scully TW, Kaur J, Panigrahi R, Belovodskiy A, Do V, Matier CD, Lemieux, M J, Wuest F, Cheeseman C, West FG.
ACS Chem Biol (2017) Apr 21;12(4):1087-1094.

Identification of Key Residues for Urate Specific Transport in Human Glucose Transporter 9 (hSLC2A9).
Long W, Panigrahi R, Panwar P, Wong K, O Neill D, Chen XZ, Lemieux MJ, Cheeseman CI.
Scientific reports (2017) 7, 41167


Full Publication list