Abstract
© 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. The segregation of cellular surfaces in heterogeneous patches is considered to be a common motif in bacteria and eukaryotes that is underpinned by the observation of clustering and cooperative gating of signaling membrane proteins such as receptors or cha nnels. Such processes could represent an important cellular strategy to shape signaling activity. Hence, structural knowledge of the arrangement of channels or receptors in supramolecular assemblies represents a crucial step towards a better understanding of signaling across membranes. We herein report on the supramolecular organization of clusters of the K + channel KcsA in bacterial membranes, which was analyzed by a combination of DNP-enhanced solid-state NMR experiments and MD simulations. We used solid-state NMR spectroscopy to determine the channel–channel interface and to demonstrate the strong correlation between channel function and clustering, which suggests a yet unknown mechanism of communication between K + channels.
Original language | English |
---|---|
Pages (from-to) | 13222-13227 |
Number of pages | 6 |
Journal | Angewandte Chemie. International Edition |
Volume | 56 |
Issue number | 43 |
DOIs | |
Publication status | Published - 2017 |
Funding
We acknowledge financial support by the NWO (700.26.121, 700.10.443, and 723.014.003).
Funders | Funder number |
---|---|
Nederlandse Organisatie voor Wetenschappelijk Onderzoek | 700.10.443, 700.26.121, 723.014.003 |
Keywords
- KcsA
- coupled gating
- dynamic nuclear polarization
- ion channels
- solid-state NMR spectroscopy