SFB 1190:  Compartmental Gates and Contact Sites in Cells

• Subject Area: Medicine ; Biology
• Term: from 2016 to 2024
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 264061860

The compartmentalization of cells ensures a highly specific distribution of nucleic acids, proteins and metabolites. At the same time, intracellular compartments must communicate and exchange molecules. Two major systems enable exchange between compartments: compartmental gates and contact sites. While compartmental gates mediate the selective partitioning of molecules between cytoplasm and organelles or within a membrane, contact sites represent direct physical connections between compartment-enclosing membranes. Thus, within living cells, compartmental gates and contact sites represent two complementary systems, which functionally cooperate or directly interact with each other to coordinate compartmentalized processes. The SFB1190 is committed to addressing the role of compartmental gates and contact sites in cellular organization and physiology. We aim to understand how they achieve a selective distribution of molecules and thus functionally define and diversify cellular compartments.

• DFG Programme: Collaborative Research Centres
• International Connection: Israel

Current projects

• P01 - Investigation of the compositional, positional and functional heterogeneity of MICOS clusters in single mammalian cells (Project Head Jakobs, Stefan )
• P03 - Maintenance and functional coupling of ER contacts with the plasma membrane (Project Head Lehnart, Stephan E. )
• P04 - The GET receptor as an entry gate to the ER and its interplay with GET bodies (Project Heads Bohnsack, Ph.D., Katherine ;  Schwappach-Pignataro, Blanche )
• P07 - Dynamics of proteins of the inner nuclear membrane (Project Head Kehlenbach, Ralph )
• P08 - Transport of large cargoes, such as ribosomal subunits, through the permeability barrier of nuclear pore complexes (Project Heads Bohnsack, Markus T. ;  Görlich, Dirk )
• P09 - Protein partitioning in the synaptic compartment: principles and molecular architecture (Project Head Rizzoli, Ph.D., Silvio-Olivier )
• P11 - Mapping cellular contact sites and their interplay (Project Head Schuldiner, Ph.D., Maya )
• P13 - Protein transport along the mitochondria carrier pathway (Project Head Rehling, Peter )
• P16 - Co-translational protein insertion into the bacterial plasma membrane (Project Head Rodnina, Marina V. )
• P17 - Exploring the role of mitochondrial contact sites on calcium and redox signaling in cancer (Project Head Bogeski, Ivan )
• P19 - Mechanism of initiating autophagosome biogenesis on ER membrane (Project Head Faesen, Alex )
• P21 - Functional role of the LDO machinery in lipid droplet-organelle contacts (Project Head Bohnert, Maria )
• P22 - Structural determinants of ER-plasma membrane contact site function (Project Head Fernandez Busnadiego, Ruben )
• P23 - Structural basis of protein transport across the outer membrane of human mitochondria (Project Head Hillen, Hauke )
• Z01 - Central Tasks of the Collaborative Research Centre (Project Head Rehling, Peter )
• Z02 - Mass spectrometry based proteomics (Project Head Urlaub, Henning )

Completed projects

• P02 - Characterization of mitochondria-ER contact sites and their role in cellular signalling (Project Heads Milosevic, Ira ;  Raimundo, Nuno )
• P06 - Relationship between organellar contact sites and autophagy in S. cerevisiae (Project Head Thumm, Michael )
• P10 - Diffusion trapping of neurotransmitter receptors at GABAergic synapses - cell biology and molecular mechanisms (Project Head Brose, Nils )
• P12 - Functional regulation of the mitochondrial presequence translocation complex (Project Head Meinecke, Michael )
• P14 - The role of human nucleoporins in the remodelling and export of macromolecular complexes (Project Head Bohnsack, Markus T. )
• P15 - Mechanisms of substrate selection in ER associated protein degradation (Project Head Stein, Alexander )
• P20 - Retrograde traffic modulates contact site formation at the ER and the Golgi (Project Head Schwappach-Pignataro, Blanche )
• Z03 - Synthetic genetic analysis, automated microscopy and image analysis (Project Head Schwappach-Pignataro, Blanche )

• Applicant Institution: Georg-August-Universität Göttingen
• Participating University: Universität Münster
• Participating Institution: Max-Planck-Institut für biophysikalische Chemie; (Karl-Friedrich-Bonhoeffer-Institut) (aufgelöst); Weizmann Institute of Science
• Spokesperson: Professor Dr. Peter Rehling