SFB 635:  Posttranslational Control of Protein Function

• Subject Area: Biology ; Medicine
• Term: from 2003 to 2015
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 5485912

After the elucidation of complete genome sequences of a number of organisms, further insight into cellular functions on the molecular level depends on the functional analysis of the expressed proteins. It is now understood that the activity of many proteins is regulated on a posttranslational level by a large variety of control mechanisms which further increase the dynamic nature of cellular proteomes and form the basis for cellular adaptation and differentiation processes. The activity of a protein can be modulated by numerous mechanisms; among them the covalent modifications of proteins, the modulation of the stability (and thereby availability) of proteins and assembly processes are emerging as major regulatory principles. Different mechanisms are frequently combined and dependent on each other. This combinatorial diversity increases the functional plasticity of regulatory networks and further calls for a collaborative approach. As posttranslational control mechanisms and components involved are often conserved, regulatory circuits are analysed in diverse organisms including bacteria, yeast, Drosophila, higher plants and mammals to unravel general regulatory principles.

• DFG Programme: Collaborative Research Centres

Completed projects

• A01 - Post-translational regulation of the activity of transcription factors that control flowering time of Arabidopsis (Project Head Coupland, Ph.D., George )
• A02 - Sorting of mono-ubiquitylated proteins in plants: Analysis of new, plant-specific sorting regulators (Project Head Hülskamp, Martin )
• A03 - Functional regulation of the clathrin adaptors (Project Head Höning, Stefan )
• A04 - Posttranslational modification and enzymatic activity of human guanylate-binding proteins (Project Head Praefcke, Gerrit )
• A05 - Functional and structural basis of the 14-3-3 mediated inhibition of plant nitrate reductase activity (Project Head Schwarz, Günter )
• A06 - Posttranslationale Modifikation des Insulin-Signaltransduktionsweges in vivo (Project Head Brüning, Jens Claus )
• A07 - Phosphotyrosine binding mediators of FGF signalling and cell junction remodelling (Project Head Leptin, Ph.D., Maria )
• A08 - Posttranslational control of MEC-2/Podocin-associated mechanosensitive ion channel complexes (Project Head Benzing, Thomas )
• A09 - Control of RhoGDIá function by post-translational lysine-acetylation (Project Head Lammers, Michael )
• A10 - Regulation of the mammalian mitochondrial ribosome by Sirt3-mediated deacetylation (Project Head Wenz, Tina )
• A11 - Post-translation control of gephyrin clustering at inhibitory synapses: phosphorylation and palmitoylation (Project Head Schwarz, Günter )
• B01 - In vivo-Proteomik des IKK-Komplexes (Project Head Pasparakis, Manolis )
• B02 - Regulatorische Wechselwirkungen der IRG-GTPasen (Project Head Howard, Jonathan Charles )
• B03 - Analysis of posttranslational modifications by a plant specific glutaredoxin (Project Head Zachgo, Sabine )
• B04 - Modes of action of the assembly factors RAR1 and SGT1 in plant disease resistance (Project Head Parker, Jane E. )
• B05 - Defining regulatory systems at the interface of protein folding and protein degradation (Project Head Höhfeld, Jörg )
• B06 - The role of UPF1 phosphorylation during nonsense-mediated mRNA decay (Project Head Gehring, Niels H. )
• B07 - Structure-function analysis of Arabidopsis EDS1 immune signalling complexes (Project Heads Niefind, Karsten ;  Parker, Jane E. )
• B08 - Control of membrane dynamics by cooperative action of bacterial dynaminlike proteins and flotillins (Project Head Bramkamp, Marc )
• C01 - Multiple mechanisms controlling the SUMO modified state of proteins (Project Head Dohmen, Jürgen )
• C02 - Functional analysis of Arabidopsis SPA proteins as co-factors of the E3 ubiquitin ligase COP1 (Project Head Höcker, Ute )
• C03 - Analysis of regulatory functions of proteasome-associated PRL1 WD-protein and SnRK1 kinases (Project Head Koncz, Csaba )
• C04 - Proteolytic control of mitochondrial biogenesis by AAA proteases (Project Head Langer, Thomas )
• C05 - Proteolytic degradation by FtsH proteases as regulatory mechanism of stress acclimatisation in cyanobacteria (Project Heads Krämer, Reinhard ;  Marin, Kay )
• C06 - Regulation of bacterial cell division by proteolysis (Project Head Bramkamp, Marc )
• C07 - From kinase activation to proteasome contributions within the plant circadian clock (Project Head Davis, Seth J. )
• C08 - Substrate recruitment and ubiquitylation by E3 ligase complexes (Project Head Hoppe, Thorsten )
• C09 - Regulation of C. elegans developmental timing by the F-box protein DRE-1/FBXO11 (Project Head Antebi, Adam )
• P04 - Phosphorylation and lipid modicication in the regulation of plant calcium-dependent protein kinases (CDPK) after biotic and abiotic stress stimuli (Project Head Romeis, Tina )
• P05 - Regulation of Arabidopsis bZIP transcription factors by phosphorylation (Project Head Harter, Klaus )
• P11 - Characterisation of the ubiquitin-protein ligase activity of the Mdm2/MdmX complex (Project Head Scheffner, Martin )
• P12 - Posttranslational control of Cyclin A turnover during the cell cycle (Project Head Sprenger, Frank )
• P17 - Proteolysis as a regulatory principle in GlnK stability and the network of nitrogen control in Corynebacterium glutamicum (Project Heads Burkovski, Ph.D., Andreas ;  Krämer, Reinhard )
• Z01 - Zentralbüro (Project Head Langer, Thomas )
• Z02 - Zentrale Proteinanalyse (Project Heads Hanisch, Franz-Georg ;  Lamkemeyer, Tobias )

• Applicant Institution: Universität zu Köln
• Participating University: Rheinische Friedrich-Wilhelms-Universität Bonn
• Spokesperson: Professor Dr. Thomas Langer