Reinhart Reithmeier

Reinhart Reithmeier


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

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.


View all publications on PubMed

Structural biology of solute carrier (SLC) membrane transport proteins.
Bai, X., Moraes, T.F. and Reithmeier, R.A.F.
2018. Mol. Memb. Biol. DOI:10.1080/09687688.2018.1448123

Band 3 function and dysfunction in a structural context.
Abbas, Y.M., Toye, A.M., Rubinstein, J.L. and Reithmeier, R.A.F.
2018. Curr. Opin. Hematol. 25, 163-170. (Invited Review) DOI: 10.1097/MOH.0000000000000418

A Ser725Arg mutation in Band 3 abolishes transport function and leads to anemia and renal tubular acidosis.
Yang, E., Seo-Mayer, P., Lezon-Geyda, K., Badior, K.E., Li, J., Casey, J.R., Reithmeier, R.A.F., Gallagher, P.G
2018. Blood 131, 1759-1763. DOI:

Molecular mechanisms of cutis laxa and distal renal tubular acidosis-causing mutations in V-ATPase a subunits, ATP6V0A2 and ATP6V0A4.
Esmail, S., Kartner, N., Yao, Y., Kim, J.W., Reithmeier, R.A.F., and Manolson, M.F.
2018. J. Biol. Chem. DOI: 10.1074/jbc.M117.818872

Molecular analysis of human solute carrier SLC26 anion transporter disease-causing mutations using 3-dimensional homology modeling.
Rapp, C., Bai, X, and Reithmeier, R.A.F.
2017. Biochim. Biophys. Acta Biomembranes 1859, 2420-2434. DOI: 10.1016/j.bbamem.2017.09.016.

N-linked Glycosylation of a Subunit Isoforms is Critical for Vertebrate Vacuolar H+-ATPase (V-ATPase) Biosynthesis.
Esmail, S., Kartner, N., Yao, Y., Kim, J.W., Reithmeier, R.A.F., and Manolson, M.F.
2017. J. Cellular Biochem. DOI: 10.1002/jcb.26250.

Effect of the Southeast Asian ovalocytosis deletion on the conformational dynamics of the signal-anchor transmembrane segment 1 of the red cell anion exchanger (AE1, Band 3, SLC4A1).
Fowler, P.W., Sansom, M.S.P. and Reithmeier, R.A.F.
2017. Biochemistry 56, 712-722. DOI: 10.1021/acs.biochem.6b00966.

Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context.
Reithmeier, R.A.F., Casey, J.R., Kalli, A.C., Sansom, M.S.P., Alguel, Y. and Iwata, S.
2016. Biochim. Biophys. Acta Biomembranes 1858, 1507-1532. (Invited Review) DOI: 10.1016/bamem.2016.03.030

N-linked glycosylation is required for vacuolar H+-ATPase (V-ATPase) a4 subunit stability, assembly and cell surface expression.
Esmail, S., Yao, Y., Kartner, N., Li, J., Reithmeier, R.A.F. and Manolson, M.F.
2016. J. Cellular Biochem. 117, 2757-2768. DOI:

Effect of SLC26 anion transporter disease-causing mutations on the stability of the homologous STAS domain of E. coli DauA (YchM).
Bai, X., Moraes, T.F. and Reithmeier, R.A.F.
2016. Biochem. J. 473, 615-626. DOI: 10.1042/BJ20151025.

Solute carriers keep on rockin’
Reithmeier, R.A.F. and Moraes, T.F.
2015. Nature Structural & Molecular Biology 22, 752–754. (News and Views) DOI: 10.1038/nsmb.3104

A call for systematic research on solute carriers.
César-Razquin, A., Snijder, B., Frappier-Brinton T., Isserlin, R., Gyimesi, G., Bai X, Reithmeier, R.A., Hepworth, D, Hediger, MA, Edwards, AM, and Superti-Furga, G.
2015. Cell 162(3), 478-87. (Perspective Article) DOI: 10.1016/j.cell.2015.07.022

Molecular dynamics simulations of the bacterial UraA H+-uracil symporter in lipid bilyaers reveal a closed state and a selective interaction with cardiolipin.
Kalli, A.C., Sansom, M.S.P. and Reithmeier, R.A.F.
2015. PLOS Comp. Biol. 11, DOI: 10.1371/journal.pcbi.1004123.

Differential roles of tryptophan residues in the functional expression of human anion exchanger 1.
Okawa, Y., Li, J., Basu, A., Casey, R.R., Reithmeier, R.A.F.
2014. Mol. Membrane Biol. 31, 211-27.

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.

Lessons from a red squirrel, Mentors, and the Pathway to Success.
Reithmeier, R.A. F.
2014. Biochem. Cell Biol. 92, 427-30.