Robert W. Mercer, Ph.D.

Cell Biology and Physiology

Molecular Cell Biology Program
Biochemistry, Biophysics, and Structural Biology Program

  • 314-362-6924

  • 314-362-6922

  • 314-362-7463

  • Room 9609 BJCIH



  • cell membrane, development, Na K-ATPase, excitable tissue, cell volume

  • Molecular and cell biology of ion pumps and transporters in plasma membrane; cell polarity

Research Abstract:

The Na,K-ATPase or sodium pump is a heterodimeric membrane protein that is responsible for maintaining the high internal potassium and low internal sodium concentrations characteristic of most animal cells. This enzyme couples the hydrolysis of ATP to the movement of sodium and potassium ions across the plasma membrane, thus producing the electrochemical gradients that are the primary source of energy for the active transport of nutrients, the action potential of excitable tissues, and the regulation of cell volume and pH.

The Na,K-ATPase consists of at least two noncovalently linked subunits: a 100 kDa multi-spanning membrane protein termed the a subunit, and the b subunit, a smaller glycosylated membrane protein. Multiple isoforms for both the a (a1-a4) and b (b1-b3) subunits have been identified. These isoforms exhibit a tissue-specific and developmental pattern of expression that may be important in the maintenance and regulation of Na,K-ATPase activity. We have also isolated and characterized the cDNAs for the g-subunit, a small hydrophobic protein associated with the other subunits. Research in this laboratory is presently directed at using the methods of molecular biology to study the structure, function, and regulation of this important enzyme.

Selected Publications:

Scheidenhelm, D.K., J. Cresswell. T.P. Fleming, R.W. Mercer and D.H. Gutmann. (2005). AKT-dependent cell size regulation by the Adhesion Molecule on Glia (AMOG) occurs independently of PI3K and Rheb signaling. Mole. Cell. Biol. 25:3151-3162.

Lansbery, K.L., L.C. Burcea, M.L. Mendenhall and R.W. Mercer. (2006). Cytoplasmic targeting signals mediate the delivery of phospholemman to the plasma membrane. Amer. J. Physiol 290:1275-4286.

Sha, Q., W. Pearson, L.C. Burcea, D.A. Wigfall, P.H. Schlesinger, C.G. Nichols, and R.W. Mercer (2008).The human FXYD2 G41R mutation responsible for renal hypomagnesemia behaves as an inward-rectifying cation channel. Amer. J. Physiol. 295:F91-F99. PMCID: 2494510

Kim, M., Habiba, A., Doherty, J.M., Mills, J.C., Mercer, R.W., and J.E. Huettner (2009). Regulation of mouse embryonic stem cell neural differentiation by retinoic acid. Dev Biol. 328:456-471. PMCID: 2666105

Nickless A, Jackson E, Marasa J, Nugent P, Mercer RW, Piwnica-Worms D, You Z (2014). Intracellular calcium regulates nonsense-mediated mRNA decay. Nat Med. 8:961-966. PMCID: PMC412686

Last Updated: 2/23/2016 8:29:38 AM

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