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Yvonne Groemping

Group leader

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Dr. Yvonne Groemping

MPI for Developmental Biology

Department of Protein Evolution

Spemannstrasse 35

72076 Tuebingen

Phone: + 49 7071 601356

Email: yvonne.groemping@tuebingen.mpg.de

 


CURRICULUM VITAE


born July 27th 1973 in Borken/Westf, Germany

two kids, Luis (*2006) and Isabel (*2009)


EDUCATION

1997-2000     Ph.D. thesis at the MPI Dortmund, Germany
1997                Diploma in biology, University of Köln, Germany
1996-1997     Diplomarbeit at the MPI Dortmund, Germany
1992-1996     Undergraduate studies in biology at the Universities of Giessen and Köln, Germany


PROFESSIONAL POSITIONS

2009-              Group leader at the MPI for Developmental Biology, Tuebingen, Germany
2005-2008     Emmy Noether group leader at the MPI for Medical Research, Heidelberg
2004                Postdoctoral fellow at the Max Planck Institute for Medical Research, Heidelberg, Germany
2001-2004     Postdoctoral fellow with Dr. Katrin Rittinger, at the NIMR, London, UK
2001                Postdoctoral fellow with Dr. Jochen Reinstein at the MPI Dortmund, Germany


GRANTS

2002-2003     Emmy Noether postdoctoral fellowship by the German Research Association (DFG). Title: Structural characterization of the NADPH oxidase.
2005-2009     Emmy Noether Junior Group leader fellowship by the German Research Association (DFG). Title: The role of adaptor proteins in regulating signaling networks.


PUBLICATIONS

Kintscher C, Wuertenberger S, Eylenstein R, Uhlendorf T, Groemping Y (2010). Autoinhibition of GEF activity in Intersectin1L is mediated by the short SH3-DH domain linker. Protein Science, 19(11):2164-74.

Rufer AC, Rumpf J, von Holleben M, Beer S, Rittinger K, Groemping Y (2009). Isoform-selective interaction of the adaptor protein Tks5/FISH with Sos1 and dynamins, J Mol Biol 390 (5): 939-50.

Kintscher C and Groemping Y (2009). Characterisation of the nucleotide exchange factor ITSN1L: Evidence for a kinetic discrimination of GEF stimulated nucleotide release from Cdc42. J Mol Biol 387 (2): 270-283.

Rumpf J, Simon B, Groemping Y, Sattler M (2008). 1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex. Biomol NMR Assign. 2 (1): 55-58.

Rumpf J, Simon B, Jung N, Maritzen T, Haucke V, Sattler M, Groemping Y. (2008). Structure of the Eps15-stonin2 complex provides a molecular explanation for EH domain ligand specificity. EMBO J. 27: 558-569.

Groemping Y, Seidel R and Reinstein J. (2005). Balance of ATPase stimulation and nucleotide exchange is not required for efficient refolding activity of the DnaK chaperone. FEBS Letters 579 (25): 5713-7.

Jozic D, Cardenes N, Deribe YL, Moncalian G, Hoeller D, Groemping Y, Dikic I, Rittinger K, Bravo J (2005). Cbl promotes clustering of endocytic adaptor proteins. Nat Struct Mol Biol 12: 972-979.

Groemping Y and Rittinger K (2005). Activation and assembly of the NADPH oxidase: a structural perspective. Biochem J 386: 401-416.

Groemping Y, Hellmann N (2005). Spectroscopic methods for the determination of protein interactions. Curr Protoc Protein Sci. Chapter 20: Unit 20.8.

Dumitru GL, Groemping Y, Klostermeier D, Restle T, Deuerling E and Reinstein J. (2004). DafA cycles between the DnaK chaperone system and translational machinery. J Mol Biol 339: 1179-89.

Groemping Y, Lapouge K, Smerdon SJ and Rittinger K (2003). Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113: 343-55.

Lapouge K, Smith SJ, Groemping Y and Rittinger K (2002). Architecture of the p40-p47-p67phox  complex in the resting state of the NADPH oxidase: A central role for p67phox. J Biol Chem 277: 10121-8.

Beinker P, Schlee S, Groemping Y, Seidel R and Reinstein J (2002). The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity. J Biol Chem 277: 47160-6.

Schlee S, Groemping Y, Herde P, Seidel R and Reinstein J (2001). Chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J Mol Biol 306: 889-99.

Groemping Y and Reinstein J (2001). Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. J Mol Biol 314: 167-78.

Groemping Y, Klostermeier D, Herrmann C, Veit T, Seidel R, Reinstein J (2001) Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. J Mol Biol 305: 1173-83.


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last modified 2011-03-01