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Journal Article

Multi-protein assemblies underlie the mesoscale organization of the plasma membrane.

MPS-Authors
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Honigmann,  A.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Eggeling,  C.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Hell,  S. W.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

2049559.pdf
(Publisher version), 4MB

Supplementary Material (public)

2049559_Suppl.pdf
(Supplementary material), 961KB

Citation

Saka, S. K., Honigmann, A., Eggeling, C., Hell, S. W., Lang T, T., & Rizzoli, S. O. (2014). Multi-protein assemblies underlie the mesoscale organization of the plasma membrane. Nature Communications, 5: 4509. doi:10.1038/ncomms5509.


Cite as: http://hdl.handle.net/11858/00-001M-0000-001A-2D1B-E
Abstract
Most proteins have uneven distributions in the plasma membrane. Broadly speaking, this may be caused by mechanisms specific to each protein, or may be a consequence of a general pattern that affects the distribution of all membrane proteins. The latter hypothesis has been difficult to test in the past. Here, we introduce several approaches based on click chemistry, through which we study the distribution of membrane proteins in living cells, as well as in membrane sheets. We found that the plasma membrane proteins form multi-protein assemblies that are long lived (minutes), and in which protein diffusion is restricted. The formation of the assemblies is dependent on ​cholesterol. They are separated and anchored by the actin cytoskeleton. Specific proteins are preferentially located in different regions of the assemblies, from their cores to their edges. We conclude that the assemblies constitute a basic mesoscale feature of the membrane, which affects the patterning of most membrane proteins, and possibly also their activity.