Reinhart Reithmeier

Reinhart Reithmeier

Professor

BSc, Carleton University, 1972
PhD, University of British Columbia, 1977
Postdoc, Harvard University, 1976-1978
Postdoc, University of Toronto, 1978-1980

Address Medical Sciences Building, Room 5368
Toronto, ON M5S 1A8
Lab Reithmeier Lab
Office Phone 416-978-7739
Email r.reithmeier@utoronto.ca

Reinhart Reithmeier obtained his B.Sc. at Carleton University in 1972 and his Ph.D. in Biochemistry at the University of British Columbia in 1977. Following post-doctoral training at Harvard and the University of Toronto he obtained his first faculty position at the University of Alberta in 1980. Dr. Reithmeier is known internationally for his research on anion transport membrane proteins in human health and disease. An award-winning lecturer, Dr. Reithmeier enjoys teaching introductory biochemistry to 1,000 undergraduate students every year, as well as upper level and graduate courses. As former Chair of Biochemistry and a Special Advisor to the Dean of Graduate Studies on graduate professional and leadership development, Dr. Reithmeier is dedicated to ensuring that graduate students have the skill set and network to be fully prepared to take advantage of the diverse job opportunities available to them in today’s global marketplace. His leadership was recognized in 2012 by election to the Canadian Academy of Health Sciences.

In the News

Research Lab

Research Description

Structure and Function of Membrane Proteins

My laboratory is interested in the structure and function of membrane proteins, in particular the chloride/bicarbonate anion exchanger (AE1, Band 3). The Band 3 glycoprotein of the erythrocyte membrane is responsible for the exchange of chloride and bicarbonate across the plasma membrane, a process necessary for respiration. A truncated form of the protein (kAE1) is expressed in the kidney where it plays an essential role in bicarbonate re-absorption.

A major aim of our research is to determine, at the molecular level, the mechanism of action of the human chloride/bicarbonate anion exchanger (AE1) and a truncated version kAE1, expressed in the kidney. We are also interested in determining the effect of mutations in the AE1 (SLC4A1) gene, linked to various hematological and kidney diseases, on the biosynthesis and function of the protein. A wide variety of structural, cellular and molecular biological techniques are employed in our research.

We have grown small 3-dimensional crystals and 2-dimensional arrays of the human Band 3 protein and we are determining its structure by X-ray diffraction and electron microscopy. A Band 3 homologue identified in yeast is being characterized with the aim of determining its structure. The structure of the cytosolic domain of normal and mutant kAE1, expressed in E. coli , is also being studied using various biophysical techniques. We are also working on the expression and crystallization of bacterial anion transporters (SLC26A/SulP) related to AE1.

We are studying the effects of mutations in Band 3 on biosynthesis and folding of this membrane protein using cell-free systems and transfected cells. We are particularly interested in the role of chaperones in mediating the proper folding and trafficking of this membrane protein. The interaction of Band 3 with glycophorin A, carbonic anhydrase, cytoskeletal and other cytosolic proteins is also a current interest. One goal is to identify the AE1 interactome, the full complement of interacting proteins using proteomics and membrane yeast 2-hybrid methods.

The interactions between various transmembrane segments in Band 3 and with the lipid bilayer is being simulated by computer modeling. Basic principles of membrane protein structure are being established by analyses of the amino acid sequences in membrane protein data banks.

Publications

View all publications on PubMed

Structure, Function and Trafficking of SLC4 and SLC26 Anion Transporters.
Cordat, E. and Reithmeier, RA.F.
2014. In Mark O. Benvensee, editor: Exchangers, Current Topics in Membranes 73, pp. 1-67, Academic Press, Elsevier Inc.

N-glycosylation and topology of the human SLC26 family of anion transport membrane proteins.
Li, J., Xia, F. and Reithmeier, R.A.F.
2014. Am. J. Physiol. 306, C943-60.

Structural and functional analysis of a putative substrate access tunnel in the cytosolic domin of human anion exchanger 1.
Shnitsar, V., Li, J., Li, X, Basu, A., Casey, J.R., Moraes, T.F., Reithmeier, R.A.F.
2013. J. Biol. Chem. 288, 33848-60.

Membrane Transport Metabolons.
Moraes, T.F. and Reithmeier, R.A.F.
2012. Biochim. Biophys. Acta Biomembranes 1818, 2687-2706.

Protein 4.2 localization and interaction with hereditary spherocytosis mutants of the cytosolic domain of human anion exchanger 1.
Bustos, S.P. and Reithmeier, R.A.F.
2011. Biochem. J. 433, 313-322.

Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism.
Babu, M., Greenblatt, J.F., Emili, A., Strynadka, N.C., Reithmeier, R.A.F. and Moraes, T.F.
2010. Cell: Structure 18, 1450-62.

Cell surface rescue of kidney anion exchanger 1 mutants by disruption of chaperone interactions.
Patterson, S.T. and Reithmeier, R.A.F.
2010. J. Biol. Chem. 285, 33423-34.