(This webpage is currently under construction)

Protein-Protein Interaction Laboratory

 Attila Reményi, PhD

Eotvos Lorand University,
Department of Biochemistry
Pázmány Péter sétány 1/C

Email: remenyi@elte.hu
Tel.: +36 1 2090555/1796 (office) or 8357 (lab)

Positions and Employment
1996-1997 Undergraduate Research (Advisor: Chris E. Dempsey) Bristol University, U.K.
1998-2001 Graduate Research (Advisor: Matthias Wilmanns, Hans Schöler) European Molecular Biology (EMBL), Germany
2002-2007 Postdoctoral Fellow (Advisor: Wendell A. Lim) University of California San Francisco (UCSF), Department of Cellular & Molecular Pharmacology, USA
2007-         Associate Research Professor, Eotvos Lorand University, Department of Biochemistry, Hungary


2006-         Leukemia & Lymphoma Society Special Fellow, USA
2002-2005 Jane Coffin Childs Memorial Fund Postdoctoral Fellowship, USA
1997-2001 EMBL Ph.D. Fellowship, Germany
1996-1997 ELTE-Bristol University Joint Scholarship, UK

Proteins are organised into networks. The outcome of many biological processess are determined by protein associations which form in a selective and dnamic manner.  We are intereted in how cellular signalling networks are organized. What molecular interactions determine the architecture of a signaling circuit? What is the molecular basis (the so-called molecular logic) underlying system-level behaviours such as promiscous or selective signal propagation, positive and negative feed-back?
In the lab we use structural biology techniques to address how cellular information is processed.

recombinant DNA techniques, protein expression and purification, X-ray structure determination, protein-protein interaction characterization, modelling

Current lab members:
Attila Reményi, PhD        associate research professor
Anita Alexa, PhD             staff scientist
Tünde Bárkai                   research associate/lab manager
Melinda Lukács               thesis student
Ágnes Garai                     thesis student


3D organization of yeast MAP-kinase modules

Specificity in kinase and protease mediated protein-protein interactions

Protein scaffolds in MAP-kinase mediated signal transduction


Reményi, A., Good, M.C., Lim, W.A. (2006) Docking interactions in protein kinase and phosphatase networks.

            Current Opinion in Structural Biology 16, 676-685

Bhattacharyya, R.P., Reményi, A., Yeh, B.J., Lim, W.A. (2006) Domains, Motifs, and Scaffolds: the role of modular interactions in the evolution and wiring of cell signalling circuits.

Annual Review of Biochemistry 75, 655-680

Bhattacharyya, R.P.*, Reményi, A.*, Good, M.C., Bashor, C, Falick, A, Lim, W.A. (2006) Ste5 allosterically modulates signaling output of the yeast mating pathway.

Science 311, 822-826 *Equal contribution

Reményi, A., Good, M.C., Bhattacharyya, R.P., Lim, W.A. (2005) The role of docking interactions in mediating signalling input, output, and discrimination in the yeast MAP kinase network.

            Molecular Cell 20, 951-952

Reményi, A., R., Schöler, H.R., Wilmanns, M. (2004) Combinatorial control of gene expression.

Nature Strucure & Molecular Biology 11, 812-815

Reményi, A., Lins, K., Nissen L.J., Reinbold, R., Schöler, H.R., Wilmanns, M. (2003) Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers.

Genes & Development 17, 2048-2059

Lins, K., Reményi, A., Tomilin, A., Massa S., Wilmanns, M, Matthias, P., Schöler, H.R. (2003) OBF1 enhances transcriptional potential of Oct1.

        EMBO Journal 22, 2188-2198

Reményi, A., Tomilin, A., Schöler, H.R., Wilmanns, M. (2002) Differential activity by DNA-induced quarternary structures of POU transcription factors.

Biochemical Pharmacology 64, 979-984

Reményi, A., Tomilin, A., Pohl, E., Lins, K., Philippsen, A., Reinbold, R., Schöler, H.R., Wilmanns, M. (2001) Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping.

Molecular Cell 8, 569-580

Reményi, A., Pohl, E., Schöler, H.R, Wilmanns, M. (2001) Crystallization of redox-insensitive Oct-1 POU domain with different DNA-response elements.

Acta Crystallographica D 57, 1634-1638

Tomilin*, A., Reményi*, A., Lins, K., Bak, H., Leidel, S., Vriend, G., Wilmanns, M., and Schöler, H. R. (2000) Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration.

Cell 103, 853-864 *Equal contribution

Takei, J., Reményi, A., Dempsey, C.E. (1999) Generalised bilayer perturbation from peptide helix dimerisation at membrane surfaces: vesicle lysis induced by disulphide-dimerised melittin analogues.

FEBS Letters 442, 11-14

Takei, J., Reményi, A., Clarke, A.R and Dempsey, C.E (1998) Self-association of disulfide-dimerized melittin analogues.

Biochemistry 37, 5699-5708