Researchers from the Ruhr-Universität Bochum (RUB) and from the MPI Dortmund have for the first time successfully reproduced the recycling process of proteins regulating cellular transport in a biophysical experiment. In doing so, they traced in detail the way the central switch protein Rab is being extracted from the lipid membrane.
The Rab protein (grey and magenta) with bound GDP (multi-coloured) sits on a membrane surface. As the infrared ray is reflected from the surface, the processes that take place on the membrane can be studied. The GDI, represented by the hand, seizes the Rab protein and extracts it from the membrane. The timeline of the infrared spectra (top centre) is resolved in the spectrometer (top right).
Credit: Konstantin Gavriljuk, RUB
The team of PD Dr Carsten Kötting, Prof Dr Klaus Gerwert (Department of Biophysics, RUB) and Prof Dr Roger S. Goody (Max Planck Institute for Molecular Physiology, Dortmund) has published the spectroscopic and dynamic data in the PNAS journal's Online Early Edition. "Until now, this protein's interactions have only ever been studied in a solution – i.e. without a lipid membrane. The step into the protein's natural environment opens up entirely new possibilities," says Carsten Kötting. This is because many disease-relevant protein interactions within a cell take place on a membrane.From solution to membrane
The project funds are supplied by SFB 642 "GTP and ATP-dependent Membrane Processes", whose spokesperson is Prof Gerwert.Bibliographic record
PD Dr Carsten Kötting, Department of Biophysics, Faculty of Biology and Biotechnology at the Ruhr-Universität, 44780 Bochum, Germany, tel. +49/234/32-24461, e-mail: Koetting@bph.rub.deA click away
Dr. Carsten Kötting | EurekAlert!
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