Understanding how the genomic information is interpreted to yield a specific phenotype is perhaps the most important question in the post-genomic era. We are investigating this by analysing protein-protein interactions and posttranslational modifications.
Proteins are the central players in this process: First, they are the final product of most genes. Therefore, understanding gene expression control requires analysis of protein synthesis and degradation. Second, function and dysfunction of proteins is directly responsible for cellular phenotypes.
Studying protein function can therefore provide novel insights into biological processes in health and disease. We are using quantitative mass spectrometry-based proteomics as our central technology to study proteome dynamics on a global scale.
The lab is interested in two major questions. First, how is the genomic information processed to yield a specific proteome? To answer this question we are studying protein synthesis and degradation. Second, how do proteins that are expressed at a specific cellular condition affect the phenotype?
- Imami K, Milek M, Bogdanow B, Yasuda T, Kastelic N, Zauber H, Ishihama Y, Landthaler M, Selbach M. Phosphorylation of the Ribosomal Protein RPL12/uL11 Affects Translation during Mitosis. Mol Cell. 2018. 72(1): 84-98.
- Meyer K, Kirchner M, Uyar B, Cheng JY, Russo G, Hernandez-Miranda LR, Szymborska A, Zauber H, Rudolph IM, Willnow TE, Akalin A, Haucke V, Gerhardt H, Birchmeier C, Kühn R, Krauss M, Diecke S, Pascual JM, Selbach M. Mutations in Disordered Regions Can Cause Disease by Creating Dileucine Motifs. Cell. 2018. 175(1):239-253.
- Zauber H, Kirchner M, Selbach M. Picky: a simple online PRM and SRM method designer for targeted proteomics. Nat Methods. 2018. 15(3):156-157.