DroPNet: a web portal for integrated analysis of Drosophila protein-protein interaction networks.

DroPNet (Drosophila Protein Network) is a Drosophila-dedicated web portal for generating and analyzing protein-protein interaction (PPI) networks. This platform integrates users' experimental data provided as one or two lists of genes with PPI data from Drosophila and other species. These experimental data can, for example, come from RNAi screens, for which this approach is known to be valuable.

The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.

Because of the importance of their physiological functions, cell membranes represent critical targets in biological research. Membrane proteins, which make up approximately 1/3 of the proteome, interact with a wide range of small ligands and macromolecular partners as well as with foreign molecules such as synthetic drugs, antibodies, toxins, or surface recognition proteins of pathogenic organisms. Whether it is for the sake of basic biomedical or pharmacological research, it is of great interest to develop tools facilitating the study of these interactions.

Monitoring the diffusion of single heterotrimeric G proteins in supported cell-membrane sheets reveals their partitioning into microdomains.

Supported cell-membrane sheets are promising in vitro systems to investigate the properties of membranes with native protein/lipid composition, in particular their sub-compartmentalization and the differential localization of proteins associated to them. While such studies are usually performed using static microscopy techniques, we demonstrate here the potential offered by dynamic diffusion measurements. Whereas the overall fluidity of the lipid bilayer was preserved, the preparation of the membrane sheets led to the selective immobilization of extracellular and transmembrane (TM) glycosylated proteins and the anchored proteins/lipids associated with them.

Cell membranes suspended across nanoaperture arrays.

We present a method for spreading large (>100 microm(2)) cell membrane fragments across nanoapertures in planar supports. Electron-beam and focused-ion-beam lithography were used to fabricate arrays of 50-600 nm diameter holes in free-standing silicon nitride (SiN) solid films 100-500 nm thick. By pressing adhering live cells onto the nanostructured SiN surface and then removing them, planar cell membrane sheets (CMSs) were transferred in a well-defined orientation onto the SiN support.

Oligomerization of the alpha 1a- and alpha 1b-adrenergic receptor subtypes. Potential implications in receptor internalization.

We combined biophysical, biochemical, and pharmacological approaches to investigate the ability of the alpha 1a- and alpha 1b-adrenergic receptor (AR) subtypes to form homo- and hetero-oligomers. Receptors tagged with different epitopes (hemagglutinin and Myc) or fluorescent proteins (cyan and green fluorescent proteins) were transiently expressed in HEK-293 cells either individually or in different combinations. Fluorescence resonance energy transfer measurements provided evidence that both the alpha 1a- and alpha 1b-AR can form homo-oligomers with similar transfer efficiency of approximately 0.