FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

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References
Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC
Voss, F. K., Ullrich, F., Münch, J., Lazarow, K., Lutter, D., Mah(*), N., Andrade-Navarro(*), M. A., von Kries, J. P., Stauber, T.; Jentsch, T. J.
Science, 344:634-638
(2014)

Tags: Physiology and Pathology of Ion Transport (Jentsch), Screening Unit (von Kries)

Abstract: Regulation of cell volume is critical for many cellular and organismal functions, yet the molecular identity of a key player, the volume-regulated anion channel VRAC, has remained unknown. A genome-wide small interfering RNA screen in mammalian cells identified LRRC8A as a VRAC component. LRRC8A formed heteromers with other LRRC8 multispan membrane proteins. Genomic disruption of LRRC8A ablated VRAC currents. Cells with disruption of all five LRRC8 genes required LRRC8A cotransfection with other LRRC8 isoforms to reconstitute VRAC currents. The isoform combination determined VRAC inactivation kinetics. Taurine flux and regulatory volume decrease also depended on LRRC8 proteins. Our work shows that VRAC defines a class of anion channels, suggests that VRAC is identical to the volume-sensitive organic osmolyte/anion channel VSOAC, and explains the heterogeneity of native VRAC currents.

Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins
Wilhelm(*), B. G., Mandad(*), S., Truckenbrodt(*), S., Kröhnert(*), K., Schäfer(*), C., Rammner(*), B., Koo, S. J., Classen, G. A., Krauss, M., Haucke, V., Urlaub(*), H.; Rizzoli(*), S. O.
Science, 344:1023-1028
(2014)

Tags: Molecular Pharmacology and Cell Biology (Haucke)

Abstract: Synaptic vesicle recycling has long served as a model for the general mechanisms of cellular trafficking. We used an integrative approach, combining quantitative immunoblotting and mass spectrometry to determine protein numbers; electron microscopy to measure organelle numbers, sizes, and positions; and super-resolution fluorescence microscopy to localize the proteins. Using these data, we generated a three-dimensional model of an "average" synapse, displaying 300,000 proteins in atomic detail. The copy numbers of proteins involved in the same step of synaptic vesicle recycling correlated closely. In contrast, copy numbers varied over more than three orders of magnitude between steps, from about 150 copies for the endosomal fusion proteins to more than 20,000 for the exocytotic ones.

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Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
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13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)
info(at)fmp-berlin.de

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