Prof. Dr. Thomas Sommer
Max-Delbrück-Center for Molecular Medicine (MDC)
Robert-Rössle-Str. 10
13125 Berlin, Germany
House 31.1, Room 4014
Phone: +49 30 9406 3753
Fax: +49 30 9406 3363
tsommer [at] mdc-berlin.de
Secretary:
Sylvia Klahn
House 31.1, Room 4012
Phone: +49 30 9406 2310
Fax: +49 30 9406 2453
klahn [at] mdc-berlin.de
Intracellular Proteolysis
Protein biogenesis is a remarkably imperfect process. About one third of all newly synthesized proteins are presumably defective. Functional proteins that were damaged by heat, oxidizing conditions or toxic agents further increase the pool of aberrant polypeptides. Defective proteins are toxic to cells and must be properly taken care of. Accordingly, cellular chaperones identify and repair deviant proteins. When salvage is not possible, the ubiquitin-proteasome pathway eliminates the faulty elements. These so-called protein quality control (PQC) pathways are found in most cellular compartments. A major PQC pathway is found in the Endoplasmic Reticulum (ER) and prevents the accumulation of malfolded or unassembled proteins in the secretory pathway. Dysfunctions in this system lead to severe diseases and, in addition, some viruses highjack this system to establish themselves in the infected cell.
Publications
Hirsch, C., Gauss, R., Horn, S.C., Neuber, O., and Sommer, T. (2009) The ubiquitylation machinery of the endoplasmic reticulum. Nature 458, 453-460.
Clerc, S., Hirsch, C., Oggier, D. M., Deprez, P., Jakob, C., Sommer, T., and Aebi, M. (2009) HTM1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J. Cell. Biol. 184, 159-172
Hirsch, C, Gauss, R, and Sommer T. (2006) Coping with stress: cellular relaxation techniques. Trends Cell Biol. 16, 657-63.
Gauss, R, Jarosch, E, Sommer, T, and Hirsch, C. (2006) A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nature Cell Biol., 8,849-854
Neuber, O., Jarosch,E., Volkwein, C., Walter, J., and Sommer, T. (2005) Ubx2/Sel1p links the Cdc48p/p97-Complex to Endoplasmic Reticulum Associated Protein Degradation. Nature Cell Biol., 7, 993-998.