Frauke Melchior Welcome to the Melchior lab!
Research in our group centers around posttranslational modification with small ubiquitin-related proteins of the SUMO family. Like ubiquitin, these proteins can be covalently and reversibly linked to other proteins. Attachment of SUMO serves to regulate protein-protein interactions, subcellular localization, enzymatic activity and stability. Projects in the lab aim at understanding mechanisms, regulation and function of SUMOylation in mammalian cells. We are interested in basic principles of reversible sumoylation (enzymes, targets and acceptor sites), connections between SUMOylation and nucleocytoplasmic transport (focusing, e.g., on the nucleoporin and E3 Ligase RanBP2/Nup358), links between SUMO- and ubiquitin-conjugation pathways, and regulation of sumoylation by redox-signaling.
Frauke Melchior will take on a new challenge - from April 1 st she joins the Board of Directors of Forschungszentrum Jülich. For more information see:
https://www.fz-juelich.de/SharedDocs/Meldungen/PORTAL/EN/2021/2021-02-1…
Frauke Melchior remains Professor at Heidelberg University and can still be contacted via her ZMBH email, but she is on leave of absence. Her research team at the ZMBH will continue until ongoing postdoc projects and PhD theses have been concluded. But we cannot recruit new lab members anymore.
Recent Research Highlights
Current Research
Research in our group centers around posttranslational modification with small ubiquitin-related proteins of the SUMO family. Like ubiquitin, these proteins can be covalently and reversibly linked to other proteins. Attachment of SUMO serves to regulate protein-protein interactions, subcellular localization, enzymatic activity and stability.
Projects in the lab aim at understanding mechanisms, regulation and function of SUMOylation in mammalian cells. We are interested in basic principles of reversible sumoylation (enzymes, targets and acceptor sites), connections between SUMOylation and nucleocytoplasmic transport (focusing, e.g., on the nucleoporin and E3 Ligase RanBP2/Nup358), links between SUMO- and ubiquitin-conjugation pathways, and regulation of sumoylation by redox-signaling.
Find out more via our recent Webinar on SUMOylation:
https://www.youtube.com/watch?v=X2AxZu05U4U
5 Selected publications
Original Papers
Schweiggert J, Habeck G, Hess S, Mikus F, Beloshistov R, Meese K, Shoji H, Knobeloch KP, Melchior F (2021). SCFFbxw5 targets kinesin-13 proteins to facilitate ciliogenesis. EMBO J, 2021;e107735.
Barysch S V, N, Stankovic-Valentin N, Miedema T, Karaca S, Doppel J, Nait Achour T, Vasudeva A, Wolf L, Sticht C, Urlaub H, Melchior F (2021). Transient deSUMOylation of IRF2BP proteins controls early transcription in EGFR signaling. EMBO Rep, 2021 Jan 22;e49651.
Stankovic-Valentin N, Drzewicka K, König C, Schiebel E, Melchior F (2016). Redox regulation of SUMO enzymes isrequired for ATM activity and survival in oxidative stress. EMBO J, 2016 Jun 15:35(12):1312-29.
Ritterhoff, T., Das, H., Hofhaus, G., Schröder, R.R., Flotho, A., and Melchior, F. (2016). The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependant nuclear export complexes. Nat Commun 7, 11482
Becker, J., Barysch, S.V., Karaca, S., Dittner, C., Hsiao, H.H., Berriel Diaz, M., Herzig, S., Urlaub, S.,Melchior, F. (2013). Detecting endogenous SUMO targets in mammalian cells and tissues. Nat. Struct. Mol. Biol 20(4):525-531.