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International PhD Program in Life Sciences - From Biological Structures to Neural Circuits

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The International Max Planck Research School for Molecular and Cellular Life Sciences (IMPRS-LS), jointly conducted by Munich based Max Planck Institutes and leading German Universities, is an internationally recognized center of scientific and educational excellence.
More than 65 distinguished group leaders actively participate in the PhD program and offer challenging and cutting-edge PhD projects in
  • Protein Structure & Protein Folding
  • Gene Regulation & DNA Biology
  • Signalling & Immunology
  • Biophysics & Multiscale Imaging
  • Computational & Systems Biology
  • Circuit Neuroscience & Neurodegeneration
The program provides comprehensive scientific training in a superb and vibrant research environment with state-of-the-art facilities. Doctoral students are fully integrated in international teams of scientists providing ample access to expertise, mentoring and support in an interdisciplinary setting.

Besides laboratory work, our students enjoy a variety of curricular activities including lectures, seminars, summer schools, elective courses, career development training and participation in international conferences.

Munich, as one of the leading German research areas in life sciences, offers a unique mixture of academic and urban lifestyle spiced with Bavarian tradition.

Highly qualified candidates with a serious commitment to basic research are invited to apply. Applicants should hold an MSc (or an equivalent degree) with a strong background in biological sciences, neurosciences, biochemistry, biophysics, biotechnology or a related discipline. Outstanding candidates with a BSc degree (or equivalent degree) are welcome to apply for the fast track option.
Successful candidates will receive a generous PhD fellowship covering living expenses and tuition.

Closing date for application is January 05, 2016; selection will be completed by March 15. Accepted candidates may start research projects as early as April 2016 and no later than October 2016.
For more information and online application please visit our website:

We offer you:
  • Excellent career opportunities in a competitive environment
  • Structured PhD program organized by Munich-based Max Planck Institutes and Universities
  • State-of-the-art facilities and cutting-edge research projects
  • Individualized supervision and mentoring
  • International setting – language of instruction is English, German language skills are not required
  • Full funding provided for international and German students
We are looking for:
  • Talented, creative and enthusiastic doctoral students from all over the world with a strong passion for science & research
The following research groups currently have job openings:

Herwig Baier: Genes – Circuits – Behavior
Thiele T, Donovan JC, Baier H (2014). Modular descending control of swim posture in zebrafish. Neuron 83: 679-691.

Roland Beckmann: Molecular Machines in Protein Targeting and Translocation
Gogala, M., Becker, T., Beatrix, B., Armache, J.P., Barrio-Garcia, C., Berninghausen, O., and Beckmann, R. (2014). Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion. Nature 506, 107-110.

Christian Biertümpfel: Molecular Mechanisms of DNA Repair
Zhao, Y., Gregory, M.T., Biertumpfel, C., Hua, Y.J., Hanaoka, F., and Yang, W. (2013).Mechanism of somatic hypermutation at the WA motif by human DNA polymerase eta.
Proc Natl Acad Sci USA 110, 8146-8151.
Tobias Bonhoeffer: Synapses- Circuits – Plasticity
Hubener, M., and Bonhoeffer, T. (2014). Neuronal Plasticity: Beyond the Critical Period.
Cell 159, 727-737.

Sigurd Braun: Regulatory Networks of Heterochromatin Formation
Braun S, Garcia JF, Rowley M, Rougemaille M, Shankar S, Madhani HD (2011). The ubiquitin ligase Cul4-Ddb1Cdt2 inhibits the invasion of a boundary-associated anti-silencing factor into heterochromatin. Cell 144, 41-54

Johannes Buchner: Protein Folding and Functional Analysis of Chaperone Proteins
Lorenz, O.R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuellar, J., Valpuesta, J. M., Madl, T., Sattler, M., and Buchner, J. (2014). Modulation of the hsp90 chaperone cycle by a stringent client protein. Mol Cell 53, 941-953.

Anne-Kathrin Classen: Proliferation, Regeneration and Morphogenesis of Epithelial Tissues
Kolybaba, A., and Classen, A.K. (2014). Sensing cellular states–signaling to chromatin pathways targeting Polycomb and Trithorax group function. Cell Tissue Res 356, 477-493

Elena Conti: Structural Studies and Molecular Mechanisms of Nucleo-Cytoplasmic Transport and mRNA Metabolism
Halbach, F., Reichelt, P., Rode, M., and Conti, E. (2013). The yeast ski complex: crystal structure and RNA channeling to the exosome complex. Cell, 154:814-826.

Jürgen Cox: Computational Systems Biochemistry
Tyanova, S., Temu, T., Carlson, A., Sinitcyn, P., Mann, M. and Cox, J. (2015) Visualization of LC-MS/MS proteomics data in MaxQuant. Proteomics 15 (8), 1453-6.

Winfried Denk: Electrons – Photons – Neurons
Helmstaedter, M., Briggman, K.L., Turaga, S.C., Jain, V., Seung, H.S., and Denk, W. (2013).
Connectomic reconstruction of the inner plexiform layer in the mouse retina. Nature 500, 168-174.

Reinhard Fässler: Integrin-Mediated Adhesion and Signalling
Rognoni, E., Widmaier, M., Jakobson, M., Ruppert, R., Ussar, S., Katsougkri, D., Bottcher, R.T., Lai-Cheong, J.E., Rifkin, D.B., McGrath, J.A., and Fassler, R. (2014). Kindlin-1 controls Wnt and TGF-beta availability to regulate cutaneous stem cell proliferation. Nat Med, 350-9.

Nadine Gogolla: Circuits for Emotion
Gogolla, N., Takesian, A.E., Feng, G., Fagiolini, M., and Hensch, T.K. (2014). Sensory integration in mouse insular cortex reflects GABA circuit maturation. Neuron 83, 894-905.

Carsten Grashoff: Mechanobiology of Cell Adhesion and Cell Division
Leerberg, J.M., Gomez, G.A., Verma, S., Moussa, E.J., Wu, S.K., Priya, R., Hoffman, B.D., Grashoff, C., Schwartz, M.A., and Yap, A.S. (2014). Tension-sensitive actin assembly supports contractility at the epithelial zonula adherens. Curr Biol 24, 1689-1699.

Oliver Griesbeck: Tools for Bio-Imaging
Litzlbauer, J., Schifferer, M., Ng, D., Fabritius, A., Thestrup, T., and Griesbeck, O. (2015). Large Scale Bacterial Colony Screening of Diversified FRET Biosensors. PLoS One 10, e0119860.

Olaf Groß: Molecular Mechanisms and Effects of Inflammasome Activation
Gross, O., Yazdi, A.S., Thomas, C.J., Masin, M., Heinz, L.X., Guarda, G., Quadroni, M., Drexler, S.K., and Tschopp, J. (2012). Inflammasome activators induce interleukin-1alpha secretion via distinct pathways with differential requirement for the protease function of caspase-1. Immunity 36, 388-400.

Ilona Grunwald Kadow: Chemosensory Coding and decision-making
Lewis L, Siju KP, Aso Y, Friedrich AB, Bulteel AJB, Rubin GM, Grunwald Kadow IC (2015). A higher brain circuit for immediate integration of conflicting sensory information in Drosophila.
Curr Biol. 31;25(17):2203-14

Christian Haass: Molecular and Cellular Mechanisms of Alzheimer’s and Parkinson’s Disease
Willem M, Tahirovic S, Busche MA, Ovsepian SV, Chafai M, Kootar S, Hornburg D, Evans LD, Moore S, Daria A, Hampel H, Müller V, Giudici C, Nuscher B, Wenninger-Weinzierl A, Kremmer E, Heneka MT, Thal DR, Giedraitis V, Lannfelt L, Müller U, Livesey FJ, Meissner F, Herms J, Konnerth A, Marie H, Haass C. (2015) η-Secretase processing of APP inhibits neuronal activity in the hippocampus.
Nature. 31. [Epub ahead of print]

F.-Ulrich Hartl: Mechanisms and Pathways of Chaperone-Mediated Protein Folding
Georgescauld, F., Popova, K., Gupta, A.J., Bracher, A., Engen, J.R., Hayer-Hartl, M., and Hartl, F.U. (2014). GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding. Cell 157, 922-934.

Reinhard Hohlfeld: Autoimmune Mechanisms and Pathogenesis of Neuroimmunological Diseases
Colombo, E., Cordiglieri, C., Melli, G., Newcombe, J., Krumbholz, M., Parada, L.F., Medico, E., Hohlfeld, R., Meinl, E., and Farina, C. (2012) Stimulation of the neurotrophin receptor TrkB on astrocytes drives nitric oxide production and neurodegeneration. J Exp Med 209, 521-535.

Karl-Peter Hopfner: Structural Biology of DNA Repair
Tosi A, Haas C, Herzog F, Gilmozzi A, Berninghausen O, Ungewickell C, Gerhold CB, Lakomek K, Aebersold R, Beckmann R, Hopfner KP. (2013). Structure and Subunit Topology of the INO80 Chromatin Remodeler and Its Nucleosome Complex. Cell, 154:1207-19.

Veit Hornung: Innate Immunity
Ablasser, A., Schmid-Burgk, J.L., Hemmerling, I., Horvath, G.L., Schmidt, T., Latz, E., and Hornung, V. (2013). Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP. Nature 503, 530-534.

Stefan Jentsch: The Function of Ubiquitin and Ubiquitin-Like Proteins
Stingele, J., Schwarz, M.S., Bloemeke, N., Wolf, P.G., and Jentsch, S. (2014). A DNA-Dependent Protease Involved in DNA-Protein Crosslink Repair. Cell 158, 549-63.

Ruediger Klein: Molecules – Signaling – Development
Seiradake, E., Del Toro, D., Nagel, D., Cop, F., Hartl, R., Ruff, T., Seyit-Bremer, G., Harlos, K., Border, E.C., Acker-Palmer, A., Jones, E.Y., and Klein, R.(2014). FLRT Structure: Balancing Repulsion and Cell Adhesion in Cortical and Vascular Development. Neuron 84, 370-385

Andreas Ladurner: Chromatin-Based Remodelling of Genome Function
Hondele, M., Stuwe, T., Hassler, M., Halbach, F., Bowman, A., Zhang, E.T., Nijmeijer, B., Kotthoff, C., Rybin, V., Amlacher, S., Hurt, E., and Ladurner, A.G. (2013). Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature, 499:111-4

Heinrich Leonhardt: Epigenetics in Development and Disease
Solovei I, Wang AS, Thanisch K, Schmidt CS, Krebs S, Zwerger M, Cohen TV, Devys D, Foisner R, Peichl L, Herrmann H, Blum H, Engelkamp D, Stewart CL, Leonhardt H and Joffe B (2013). LBR and Lamin A/C Sequentially Tether Peripheral Heterochromatin and Inversely Regulate Differentiation. Cell, 152, 584-598

Stefan Lichtenthaler: Neurodegeneration, Proteases, Neuroproteomics
Hogl S, van Bebber F, Dislich B, Kuhn PH, Haass C, Schmid B, Lichtenthaler SF (2013). Label-free quantitative analysis of the membrane proteome of Bace1 protease knock-out zebrafish brains. Proteomics 13, 1519-1527.

Matthias Mann: Proteomics and Signal Transduction
Humphrey, S. J.; Azimifar, S. B.; Mann, M.: (2015). High-throughput phosphoproteomics reveals in vivo insulin signaling dynamics. Nature Biotechnology, 33 (9),

Felix Meissner: Experimental Systems Immunology
Meissner, F., Scheltema, R.A., Mollenkopf, H.J., and Mann, M. (2013). Direct proteomic quantification of the secretome of activated immune cells. Science, 340:475-478.

Juerg Mueller: Chromatin and Transcription in Development
Pengelly, A.R., Copur, O., Jackle, H., Herzig, A., and Muller, J. (2013). A histone mutant reproduces the phenotype caused by loss of histone-modifying factor Polycomb. Science, 339:698-699.

Andreas Pichlmair: Innate Recognition of Viruses and the Cellular Antiviral Defence
Habjan, M., Hubel, P., Lacerda, L., Benda, C., Holze, C., Eberl, C.H., Mann, A., Kindler, E., Gil-Cruz, C., Ziebuhr, J., Thiel, V., and Pichlmair, A. (2013). Sequestration by IFIT1 Impairs Translation of 2’O-unmethylated Capped RNA. PLoS Pathog 9, e1003663.

Jürgen Ruland: Molecular Mechanisms of Immune Cell Activation
Neumann, K., Castineiras-Vilarino, M., Hockendorf, U., Hannesschlager, N., Lemeer, S., Kupka, D., Meyermann, S., Lech, M., Anders, H.J., Kuster, B., Busch, D.H., Gewies, A., Naumann, R., Gross, O., and Ruland, J. (2014). Clec12a Is an Inhibitory Receptor for Uric Acid Crystals that Regulates Inflammation in Response to Cell Death. Immunity 40, 389-399.

Michael Sattler: Structural Basis of Protein-Protein & Protein-RNA Interactions in the Regulation of Gene Expression
Hennig, J. Militti, C., Popowicz, G.M., Wang, I., Sonntag, M., Geerlof, A., Gabel, F., Gebauer, F., and Sattler, M. (2014). Structural basis for the assembly of the Sxl-Unr translation regulatory complex. Nature. 13;515(7526):287-90

Marc Schmidt-Supprian: Signal Transduction During Immune Reactions and Lymphomagenesis
Vahl, J.C., Drees, C., Heger, K., Heink, S., Fischer, J.C., Nedjic, J., Ohkura, N., Morikawa, H., Poeck, H., Schallenberg, S., Riess, D., Hein, M.Y., Buch, T., Polic, B., Schonle, A., Zeiser, R., Schmitt-Graff, A., Kretschmer, K., Klein, L., Korn, T., Sakaguchi, S., and Schmidt-Supprian, M. (2014) Continuous T Cell Receptor Signals Maintain a Functional Regulatory T Cell Pool.
Immunity 41, 722-736.

Petra Schwille: Cell and Membrane Biophysics
Arumugam, S., Petrasek, Z., and Schwille, P. (2014) MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulation. Proc Natl Acad Sci U S A 111, E1192-1200.

Jürgen Soll: Protein Transport Across the Chloroplast Membrane
Lintala, M., Schuck, N., Thormahlen, I., Jungfer, A., Weber, K.L., Weber, A.P., Geigenberger, P., Soll, J., Bolter, B., and Mulo, P. (2014) Arabidopsis tic62 trol mutant lacking thylakoid-bound ferredoxin-NADP+ oxidoreductase shows distinct metabolic phenotype. Mol Plant 7, 45-57.

Julia von Blume: Molecular Basis of Protein Trafficking
Kienzle, C., Basnet, N., Crevenna, A.H., Beck, G., Habermann, B., Mizuno, N., and von Blume, J. (2014) Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting.
J Cell Biol 206, 635-654

Thomas Wollert: Molecular Membrane and Organelle Biology
Kaufmann, A., Beier, V., Franquelim, H.G., and Wollert, T. (2014). Molecular mechanism of autophagic membrane-scaffold assembly and disassembly. Cell 156, 469-481.

Wolfgang Zachariae: Control of Chromosome Segregation in Meiosis
Okaz, E., Arguello-Miranda, O., Bogdanova, A., Vinod, P.K., Lipp, J.J., Markova, Z., Zagoriy, I., Novak, B., and Zachariae, W. (2012) Meiotic Prophase Requires Proteolysis of M Phase Regulators Mediated by the Meiosis-Specific APC/C(Ama1). Cell 151, 603-618.


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Dr. Hans-Joerg Schaeffer
MPI of Biochemistry
Am Klopferspitz 18
82152 Munich-Martinsried

Details der Stellenanzeige

Befristete Anstellung
Berufserfahrung nicht vorausgesetzt
Deutschland (Bayern)
82152 Munich-Martinsried
Biologie & Life Sciences, Chemie, Physik