个人简介

Diploma in Chemistry (equivalent to M.S.), Johann Wolfgang Goethe-University, Frankurt, Germany, 1990 Ph.D. in Physical Chemistry, Johann Wolfgang Goethe-University, Frankfurt, Germany, 1993

研究领域

Biological and Physical Chemistry

The long-term goal of our research is to understand the function and the working mechanism of membrane-bound transport proteins. In general, transporters use different types of energy sources to actively move specific substrates, such as inorganic ions or small, organic molecules across the membrane into or out of cells. Recently, significant progress has been made towards our understanding of the molecular architecture through the availability of high-resolution structures of several transporters. However, the actual transport mechanism(s) remain elusive. Our aim is to combine functional and structural evidence in order to obtain an understanding of how these transport proteins work.

近期论文

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Sequence Selective Recognition of Double-Stranded RNA at Physiologically Relevant Conditions Using PNA-Peptide Conjugates. Muse O, Zengeya T, Mwaura J, Hnedzko D, McGee DW, Grewer C, Rozners E. ACS Chem. Biol. (2013) 16:1683-1686. Voltage-dependent processes in the electroneutral amino acid exchanger ASCT2. Zander CB, Albers T, Grewer C. J. Gen. Physiol. (2013) 141:659-672 Electrophysiological characterization of membrane transport proteins. Grewer C, Gameiro A, Mager T, Fendler K. Annu. Rev. Biophys. (2013) 42:95-120. Protonation state of a Conserved acidic amino acid involved in Na+ binding to the glutamate transporter EAAC1. Mwaura J, Tao Z, James H, Albers T, Schwartz A, Grewer C. ACS Chem. Neurosci. (2012) 19:1073-1083 Grewer C, Zhang Z, Mwaura J, Albers T, Schwartz A, Gameiro A. Charge compensation mechanism of a Na+-coupled, secondary active glutamate transporter. J. Biol. Chem. (2012) 287:26921-26931. Callender R, Gameiro A, Pinto A, De Micheli C, Grewer C. Mechanism of Inhibition of the Glutamate Transporter EAAC1 by the Conformationally Constrained Glutamate Analogue (+)-HIP-B. Biochemistry (2012) 51:5486-5495. Albers T, Marsiglia W, Thomas T, Gameiro A, Grewer C. Defining substrate and blocker activity of alanine-serine-cysteine transporter 2 (ASCT2) Ligands with Novel Serine Analogs. Mol. Pharmacol. (2012) 81:356-365. Gameiro, A., Braams, S., Rauen, T., and Grewer, C. The Discovery of Slowness: Low capacity transport and slow anion channel gating by the glutamate transporter EAAT5, Biophys. J. (2011) 100; 2623-2632. Zhang, Z., Zander, C. B. and Grewer, C. The C-terminal domain of the neutral amino acid transporter SNAT2 regulates transport activity through voltage-dependent processes, Biochem. J. (2011) 434; 287-296 Tao, Z., Rosental, N., Kanner, B. I., Gameiro, A., Mwaura, J., Grewer, C. Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue T101. J. Biol. Chem. (2010) 285; 17725-17733 Zhang, Z., Albers, T., Fiumera, H. L., Gameiro, A., and Grewer, C. A conserved Na+ binding site of the sodium-coupled neutral amino acid transporter 2 (SNAT2). J. Biol. Chem. (2009) 284; 25314-25323 Zhang, Z, Gameiro, A, and Grewer, C. "Highly-conserved asparagine 82 controls the interaction of Na+ with the sodium-coupled neutral amino acid transporter SNAT2.", J. Biol. Chem., (2008), 283, 12284-12292 Erreger, K., Grewer, C., Javitch, J. A. and Galli, A., "Currents in response to rapid concentration jumps of amphetamine uncover novel aspects of human dopamine transporter function.", J. Neurosci., (2008), 28, 976-989 Zhang, Z., Tao, Z., Gameiro, A., Barcelona, S., Braams, S., Rauen, T. and Grewer, C., "The transport direction determines the kinetics of substrate transport by the glutamate transporter EAAC1.", Proc. Natl. Acad. Sci. USA, (2007), 104, 18025-18030 Zhang, Z. and Grewer, C., "The sodium-coupled neutral amino acid transporter SNAT2 mediates an anion leak conductance that is differentially inhibited by transported substrates." Biophys. J., (2007), 92, 2621-2632 Maier, W., Schemm, R., Grewer, C., and Laube, B., "Disruption of interdomain interactions in the glutamate binding pocket affects differentially agonist affinity and efficacy of NMDA receptor activation." J. Biol. Chem., (2007), 282, 1863-1872 Tao, Z., Zhang, Z., and Grewer, C., "Neutralization of the aspartic acid residue D367, but not D454, inhibits binding of Na+ to the glutamate-free form and cycling of the glutamate transporter EAAC1." J. Biol. Chem., (2006), 281, 10263-10272 Mim C, Balani P, Rauen T, and Grewer C., "The Glutamate Transporter Subtypes EAAT4 and EAATs 1-3 Transport Glutamate with Dramatically Different Kinetics and Voltage Dependence but Share a Common Uptake Mechanism.", J. Gen. Physiol., (2005), 126, 571-589 Grewer, C. Watzke, N., Rauen, T. and Bicho, A., "Is the Glutamate Residue E373 the Proton Sensor of the Glutamate Transporter EAAC1?", J. Biol. Chem., (2003),278, 1585-2592 Watzke, N., Bamberg, E. and Grewer, C., "Early Intermediates in the Transport Cycle of the Neuronal Excitatory Amino Acid Carrier EAAC1.", J. Gen. Physiol., (2001), 117, 547-562. This article was featured on the cover of this JGP issue.