Protein Quality Control in the Secretory Pathway

Öffentlicher Abendvortrag

The ubiquitin proteasome system is a major device found in all eucaryotic cells. It specifically recognizes proteins that are not needed anymore or proteins that are damaged. These targets are labeled with the small protein ubiquitin. Proteins labeled with ubiquitin are subsequently digested by a huge protease termed the proteasome. The elimination of damaged proteins is of particular interest, since misfolded proteins have the tendency to form aggregates inside cells which can cause damage and lead to disorders like neurodegenerative diseases. Collectively these cellular pathways involved in recognition and elimination of damaged proteins are called protein quality control (PQC) pathways. Today we know that they are found in all cellular compartments, but the best-studied example is that of the secretory apparatus.
Thomas Sommer has studied biology at the Free University of Berlin. He performed the experimental part of his doctoral thesis at the Max-Planck-Institute for Molecular Genetics in Berlin and received his degree in 1988 from the FU Berlin. Later he joined the laboratory of Stefan Jentsch at the Friedrich Miescher Institute of the Max-Planck-Society in Tübingen as a Postdoc. During his stay he discovered components of the ubiquitin proteasome system that are involved in protein quality control. In 1993 he joined the Max-Delbrück-Center for Molecular Medicine (MDC) in Berlin Buch as a junior group leader and became permanent faculty member in 1999. Since 2004 he is vice scientific director of the MDC and since 2009 in addition a professor for cellular biochemistry at the Humboldt-University of Berlin.
Moderation: Professor Dr. Barbara M. Bröker


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