Project Details
SFB 807: Transport and Communication across Biological Membrans
Subject Area
Biology
Chemistry
Chemistry
Term
from 2008 to 2020
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 57566863
Biological membranes are intimately associated with the evolution of life, providing a barrier to or within the cell that allows for compartmentalisation and structure formation as well as concentration of molecules. However, any living cell has to communicate via this barrier with its environment and, therefore, membranes are equipped with a multitude of membrane proteins that are required for uptake and export of molecules and for communication across this barrier (sensing of stimuli and signal transduction to intracellular targets). This pivotal role of membrane proteins is exemplified in genomes from all kingdoms of life, in which 25-30 percent of the genetic information encodes for membrane proteins. Despite their importance for the physiology of cells, a precise understanding of membrane proteins and processes are only rarely available. In particular, transport processes and information transfer are often not well resolved, even though they are of paramount interest from a biomedical standpoint of view as reflected by the fact that roughly 60 percent of the currently used medical drugs target transmembrane processes. This discrepancy between our knowledge and the importance of transmembrane processes will ensure that this research area will stay in the focus both of academic research as well as the pharmaceutical industry for years to come. The Collaborative Research Centre is designed to be a comprehensive multidisciplinary approach to study the principles and molecular mechanisms of transport of molecules and information across membranes in different cellular systems and subcellular compartments. The consortium combines a large set of biochemical, biophysical, cell and structural biological as well as computational approaches to elucidate these processes in molecular detail. This entails the determination of the chronological order of key events during a transfer cycle, their timescales and their structural bases. In particular, the presumed ability of transporters and receptors to adopt multiple conformations, which are required for completion of a full activity cycle, requires the identification of these essential conformational states and an understanding of how interchange between them occurs. We will address how these events are integrated into macromolecular complexes and signalling networks by analysing their crosstalk with other membrane proteins as well as with intra- and extracellular factors.
DFG Programme
Collaborative Research Centres
Completed projects
- MGK - Integrated Research Training Group (Project Head Pos, Klaas Martinus )
- P01 - Structure and mechanisms of membrane transport proteins (Project Head Kühlbrandt, Werner )
- P02 - Cell-free synthesized G-protein coupled receptors in synthetic membranes and other hydrophobic environments (Project Heads Bernhard, Frank ; Dötsch, Volker )
- P03 - Structural genomics on selected families of secondary active transporters (Project Head Michel, Hartmut )
- P04 - Dynamic molecular description of transport regulation in BetP (Project Head Ziegler, Christine Maria )
- P05 - Structural properties, activation mechanisms and transport processes in betaine transporter BetP and Na+/H+ antiporters NhaA/MjNhaP1 investigated by FT-IR and CD spectroscopy (Project Head Mäntele, Werner )
- P06 - The mechanism of primary-active transporters, light-driven ion channels and pumps studied by solid-state NMR (Project Head Glaubitz, Clemens )
- P07 - Dipolar EPR spectroscopy on membrane embedded transport complexes (Project Heads Joseph, Ph.D., Benesh ; Prisner, Thomas F. )
- P08 - Computational studies of alternating access mechanisms in sodium-dependent secondary transporters (Project Head Forrest, Lucy )
- P09 - Function and mechanism of the lysosomal polypeptide transporter ABCB9 (Project Head Abele, Rupert )
- P10 - Light gated ion channels and secondary active transporters: mechanism and application (Project Heads Bamberg, Ernst ; Fendler, Klaus )
- P11 - Microbial rhodopsins as optogenetic tools to analyze neuronal networks in the nematode Caenorhabditis elegans (Project Head Gottschalk, Alexander )
- P12 - Photo-initiated functional dynamics of retinal proteins (Project Heads Bamann, Christian ; Wachtveitl, Josef )
- P13 - NMR investigations of retinal binding proteins (Project Head Schwalbe, Harald )
- P14 - SFunction, subunit composition, and structure of archaeal ATP synthases (Project Head Müller, Volker )
- P15 - Structure and function of bacterial ATP synthases (Project Head Meier, Thomas )
- P16 - Translocation mechanism of ABC exporters and the peptide-loading complex (Project Head Tampé, Robert )
- P17 - Structure, function, and dynamics of the TOC core complex (Project Head Schleiff, Enrico )
- P18 - Struktur-Funktions-Beziehung von dreiteiligen Arzneimittel-auswärtspumpenden RND-Komplexen s (Project Head Pos, Klaas Martinus )
- P19 - Structural organization of macro-molecular complexes in membranes: The MHC class I peptide-loading complex (Project Head Schäfer, Lars )
- P20 - Conformational dynamics and communication of membrane transporters and receptors studied at the single-molecule level in vitro and in vivo (Project Head Heilemann, Mike )
- P21 - Activation mechanism of the unfolded protein response by lipid bilayer stress (Project Head Ernst, Robert )
- P22 - Functional modulation of the K+ transporter KtrAB in vivo and in vitro (Project Head Hänelt, Inga )
- P23 - Structure, function, and dynamics of SLC26 and NCS2 transporters (Project Head Geertsma, Eric )
- P24 - Dynamics of complex membrane assemblies probed by native mass spectrometry (Project Head Morgner, Nina )
- P25 - Atomistic simulation and modeling of active membrane transport (Project Head Hummer, Gerhard )
- Z01 - Central Tasks of the Collaborative Research Center (Project Head Tampé, Robert )
Applicant Institution
Goethe-Universität Frankfurt am Main
Participating Institution
Max-Planck-Institut für Biophysik
Spokesperson
Professor Dr. Robert Tampé