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Matthias Voss
Haass Lab
Room 804, Adolf-Butenandts Institute & German Center for Neurodegenerative Diseases (DZNE) - Munich, Schillerstraße 44, Munich
+89 2180 75 464
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Intramembrane proteolysis of transmembrane proteins following their initial ectodomain shedding serves as a mechanism for intracellular release of functional protein moieties and membrane protein degradation. Notably, this process is implicated in the pathogenesis of a number of human diseases, including chronic inflammatory disease, flavivirus infection and, in particular, Alzheimer’s disease. Among the intramembrane cleaving proteases the presenilins, the active site containing subunits of the γ-secretase complex, the signal peptide peptidase (SPP) and signal peptide peptidase-like (SPPL) form a family of aspartate proteases that share a common GxGD motif at their active site.
In this thesis, the molecular basis of enzyme-substrate interaction of these GxGD-type proteases will be investigated. By construction of various SPPL mutants and swap variants with SPP, SPPL3 and also presenilin domains, enzyme-substrate interactions and substrate specificity will be analyzed. This may allow me to determine which enzyme domains contribute to substrate recognition and in particular the selectivity for type II transmembrane protein substrates observed in SPPLs.


  • Graduate program "Protein Dynamics in Health and Disease", Elite Network of Bavaria (since 09/2009)
  • Graduate program "Neurodegenerative Disease Research, SFB 596, Ludwig-Maximilians University Munich, SPP/SPPL group, Prof. Dr. Ch. Haass & PD Dr. R. Fluhrer, Adolf-Butenandt-Institute, LMU Munich & German Center for Neurodegenerative Diseases (DZNE) - Munich (since 04/2009)
  • Diploma thesis: "The FasL/SH3 domain interactome: Identification of novel interactions partners of the N-terminus of human FasL", Prof. Dr. O. Janssen, Institute of Immunology, University Medical Center Schleswig-Holstein, Campus Kiel (03/2009)
  • Diploma program "Biochemistry and Molecular Biology", Christian-Albrechts University, Kiel (10/2004 to 03/2009)
  • Student assistant, Prof. Dr. K. Reiss & Prof. Dr. P. Saftig, Institute of Biochemistry, Christian-Albrechts University, Kiel (10/2006 to 06/2007)
  • Student assistant, PD Dr. A. Ludwig, Institute of Biochemistry, Christian-Albrechts University, Kiel (2005-2006)


Voss M, Fukumori A, Kuhn PH, Künzel U, Klier B, Grammer G, Haug-Kröper M, Kremmer E, Lichtenthaler SF, Steiner H, Schröder B, Haass C, Fluhrer R (2012). Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3). J Biol Chem 287, 43401-43409.

Schwarz, N., Pruessmeyer, J., Hess, M.F., Pantaler, E., Windoffer, R., Voss, M., Sarabi, A., Sechi, A., Uhlig, S., Ludwig, A. (2010). Sequential steps of leukocyte recruitment via the transmembrane chemokine CX3CL1. Cell Mol Life Sci 67, 4233-4248.

Lettau, M., Pieper, J., Gerneth, A., Lengl-Janßen, B., Voss, M., Linkermann, A., Schmidt, H., Gelhaus, C., Leippe, M., Kabelitz, D., Janssen, O. (2010). The adapter protein Nck: Role of individual SH3 and SH2 binding modules for protein interactions in T lymphocytes. Protein Sci 19, 658-669.

Voss, M.*, Lettau, M.*, Janssen, O. (2009). Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening. BMC Immunol 10, 53.

Voss, M.*, Lettau, M.*, Janssen, O. (2008). Posttranslational regulation of FasL function. Cell Commun Signal 6, 11.


Talks:

Voss, M., Haass, C., Fluhrer R. (2011). Molecular Characterization of Signal Peptide Paptidase-like Protease 3. (Talk at the Protease Winter School, Tiers, Italy, February 23rd to 27th)


Posters:

Lettau, M.*, Voss, M.*, Janssen, O. (2009). Differential binding of Fas ligand-interacting proteins to the full length protein or N-terminal fragments generated by shedding. (13th Signal Transduction Society Meeting 2008, Weimar, October 28th-30th)

Lettau, M. *, Pieper, J., Lengl-Janßen, B., Voss, M., Gelhaus, C., Leippe, M., Janssen, O. (2009). SH2/SH3 interaction partners of Nck in human T cells. (13th Signal Transduction Society Meeting 2008, Weimar, October 28th-30th)

Voss, M.*, Lettau, M.*, Janssen, O. (2009): Proteome-wide screening of SH3 domain interaction partners for the proline-rich region of FasL. (2nd European Congress of Immunology, Berlin, September 13th-16th.)

Lettau, M. *, Pieper, J.*, Lengl-Janßen, B., Voss, M., Gelhaus, C., Leippe, M., Janssen, O. (2009): The Nck interactome in T cells. (2nd European Congress of Immunology, Berlin, September 13th-16th.)

Voss, M., Janssen, O., Lettau, M. (2009): Identification of SH3 domain interaction partners of FasL using a human SH3 domain phage display library. Cell Commun Signal 7 (Suppl 1), A92. (12th Signal Transduction Society Meeting 2008, Weimar, October 29th-31st)

Pieper, J., Lengl-Janßen, B., Voss, M., Gelhaus, C., Leippe, M., Janssen, O., Lettau M. (2009): Identification of interactions partners of the adapter protein Nck in T cells. Cell Commun Signal 7 (Suppl 1), A84. (12th Signal Transduction Society Meeting 2008, Weimar, October 29th-31st)

*equal contribution


  • PhD fellowship, Hans und Ilse Breuer Stiftung (since 01/2010)
  • Diploma award, German Society for Biochemistry and Molecular Biology (GBM) (10/2009)
  • e-fellows.net online scholarship (since 04/2009)
  • Travel grant, Signal Transduction Society (10/2008)
  • “Holstein” study award, Christian-Albrechts University of Kiel (02/2008)
  • Scholarship of the Studienstiftung des deutschen Volkes (03/2007 to 03/2009)



Signal Transduction Society (STS)

Gesellschaft für Biochemie und Molekularbiologie (GBM) e.V.

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Matthias Voss
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