SFB 1507:  Protein Assemblies and Machineries in Cell Membranes

• Subject Area: Biology ; Medicine
• Term: since 2022
• Website: Homepage
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 450648163

Protein assemblies and molecular machineries in cellular membranes are central to essential life processes. They establish homeostasis in compartmentalized cells, transduce energy, translocate nutrients and metabolites, control the communication within and between cells, and mediate interactions with pathogens. The CRC aims for an in-depth, quantitative understanding of the structure, dynamics, and function of key membrane-associated assemblies, machineries, and supercomplexes as a basis for a multiscale decoding of the associated cellular processes. Despite their pivotal role, protein assemblies and machineries associated with cellular membranes are intrinsically difficult to study and remain poorly understood. Our CRC aims to discover the organizational principles and operational mechanisms of protein assemblies and machineries at and across compartmentalization boundaries.The CRC projects are thematically intertwined and take full advantage of the many advanced methodologies and emerging techniques available through the CRC members. Each project is based on uniform principles and focuses on central topics to elucidate the role and modular organization of functional units confined in membranes. The CRC projects also interlock in the innovative use of integrative in vitro and in situ approaches, ranging from cryo-electron microscopy, X-ray crystallography, magnetic resonance spectroscopy, and high-resolution light microscopy, to native mass spectrometry, ultrafast spectroscopy, optogenetics, and artificial intelligence (AI)-guided molecular dynamics simulations and modelling. In summary, the close thematic and methodological connections between the groups and their tight interactions place this CRC into a unique position to uncover fundamental principles of membrane protein assemblies in cell compartmentalization that are conserved between different cells and organisms.

• DFG Programme: Collaborative Research Centres

Current projects

• MGK - Integrated Research Training Group (Project Head Hänelt, Inga )
• P01 - Insights into lipopolysaccharide (LPS) transport by solid-state NMR spectroscopy (Project Head Glaubitz, Clemens )
• P02 - Mechanism of bacterial transenvelope protein and lipid transport (Project Head Joseph, Ph.D., Benesh )
• P03 - Molecular basis of lipid transport across the periplasm (Project Head Pos, Klaas Martinus )
• P04 - Regulation of potassium channel YugO in bacterial electrical signaling (Project Head Hänelt, Inga )
• P05 - Molecular dynamics of light responsive molecular machines (Project Head Wachtveitl, Josef )
• P06 - Optogenetic analysis of membrane compartmentalization between and within excitable cells (Project Head Gottschalk, Alexander )
• P07 - Dynamics of membrane receptor clustering in endothelial cells (Project Head Acker-Palmer, Amparo )
• P08 - Quantitative super-resolution microscopy unravels nanoscale patterns of membrane receptor networks (Project Head Heilemann, Mike )
• P09 - Artificial intelligence-guided molecular dynamics simulations decipher the activation mechanism of cellular control programs (Project Head Covino, Roberto )
• P10 - Modulation of tyrosine receptor signaling investigated by NMR spectroscopy (Project Head Schwalbe, Harald )
• P11 - Structure and dynamics of the TRPV4 ion channel as a cellular signaling hub (Project Head Hellmich, Ute )
• P12 - Molecular dynamics simulations of membrane perforation machineries and the nuclear pore complex (Project Head Hummer, Gerhard )
• P13 - Probing multiprotein assemblies with native mass spectrometry (Project Head Morgner, Nina )
• P14 - Structural basis of complex I function and assembly (Project Heads Vonck, Janet ;  Zickermann, Volker )
• P15 - Structure and mechanism of membrane-bound hydrogenases (Project Head Murphy, Ph.D., Bonnie J. )
• P16 - Dissecting the role of SND pathway components in ER membrane protein insertion (Project Head McDowell, Melanie )
• P17 - Understanding nuclear pore complexity (Project Heads Beck, Martin ;  Lemke, Edward A. )
• P18 - Protein assemblies and machineries in antigen processing and ER quality control (Project Head Tampé, Robert )
• Z01 - Central Tasks of the Collaborative Research Center (Project Head Tampé, Robert )
• Z02 - Single-particle cryo-EM infrastructure (Project Heads Beck, Martin ;  Tampé, Robert )

• Applicant Institution: Goethe-Universität Frankfurt am Main
• Participating Institution: Max-Planck-Institut für Biophysik ; Abteilung Theoretische Biophysik; Frankfurt Institute for Advanced Studies (FIAS)
• Participating University: Friedrich-Schiller-Universität Jena; Johannes Gutenberg-Universität Mainz
• Spokesperson: Professor Dr. Robert Tampé