Bilayer-mediated clustering and functional interaction of MscL channels

Grage, Stephan L., Keleshian, Asbed M., Turdzeladze, Tamta, Battle, Andrew R., Tay, Wee C., May, Roland P., Holt, Stephen A., Contera, Sonia Antoranz, Haertlein, Michael, Moulin, Martine, Pal, Prithwish, Rohde, Paul R., Forsyth, V. Trevor, Watts, Anthony, Huang, Kerwyn Casey, Ulrich, Anne S. and Martinac, Boris (2011) Bilayer-mediated clustering and functional interaction of MscL channels. Biophysical Journal, 100 5: 1252-1260. doi:10.1016/j.bpj.2011.01.023


Author Grage, Stephan L.
Keleshian, Asbed M.
Turdzeladze, Tamta
Battle, Andrew R.
Tay, Wee C.
May, Roland P.
Holt, Stephen A.
Contera, Sonia Antoranz
Haertlein, Michael
Moulin, Martine
Pal, Prithwish
Rohde, Paul R.
Forsyth, V. Trevor
Watts, Anthony
Huang, Kerwyn Casey
Ulrich, Anne S.
Martinac, Boris
Title Bilayer-mediated clustering and functional interaction of MscL channels
Journal name Biophysical Journal   Check publisher's open access policy
ISSN 0006-3495
1542-0086
Publication date 2011-03-02
Sub-type Article (original research)
DOI 10.1016/j.bpj.2011.01.023
Volume 100
Issue 5
Start page 1252
End page 1260
Total pages 9
Place of publication St. Louis, MO, United States
Publisher Cell Press
Language eng
Abstract Mechanosensitive channels allow bacteria to respond to osmotic stress by opening a nanometer-sized pore in the cellular membrane. Although the underlying mechanism has been thoroughly studied on the basis of individual channels, the behavior of channel ensembles has yet to be elucidated. This work reveals that mechanosensitive channels of large conductance (MscL) exhibit a tendency to spatially cluster, and demonstrates the functional relevance of clustering. We evaluated the spatial distribution of channels in a lipid bilayer using patch-clamp electrophysiology, fluorescence and atomic force microscopy, and neutron scattering and reflection techniques, coupled with mathematical modeling of the mechanics of a membrane crowded with proteins. The results indicate that MscL forms clusters under a wide range of conditions. MscL is closely packed within each cluster but is still active and mechanosensitive. However, the channel activity is modulated by the presence of neighboring proteins, indicating membrane-mediated protein-protein interactions. Collectively, these results suggest that MscL selfassembly into channel clusters plays an osmoregulatory functional role in the membrane.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biomedical Sciences Publications
 
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