Crystalline Protein Domains and Lipid Bilayer Vesicle Shape Transformations
Name
Horton-2007-Crystalline Protein Domains.pdf
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Author(s)
Gast, Alice Petry
Horton, Margaret R.
Manley, Suliana
Arevalo, Silvana R.
Lobkovsky, Alexander E.
Date Issued
January 2007
Journal
Journal of Physical Chemistry B
Publisher
American Chemical Society (ACS)
Citation
Horton, Margaret R. et al. “Crystalline Protein Domains and Lipid Bilayer Vesicle Shape Transformations.” The Journal of Physical Chemistry B 111.4 (2007): 880–885. Web. 12 Apr. 2012. © 2007 American Chemical Society
Version
Final published version
Abstract
Cellular membranes can take on a variety of shapes to assist biological processes including endocytosis. Membrane-associated protein domains provide a possible mechanism for determining membrane curvature. We study the effect of tethered streptavidin protein crystals on the curvature of giant unilamellar vesicles (GUVs) using confocal, fluorescence, and differential interference contrast microscopy. Above a critical protein concentration, streptavidin domains align and percolate as they form, deforming GUVs into prolate spheroidal shapes in a size-dependent fashion. We propose a mechanism for this shape transformation based on domain growth and jamming. Osmotic deflation of streptavidin-coated GUVs reveals that the relatively rigid streptavidin protein domains resist membrane bending. Moreover, in contrast to highly curved protein domains that facilitate membrane budding, the relatively flat streptavidin domains prevent membrane budding under high osmotic stress. Thus, crystalline streptavidin domains are shown to have a stabilizing effect on lipid membranes. Our study gives insight into the mechanism for protein-mediated stabilization of cellular membranes.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
Massachusetts Institute of Technology. Department of Earth, Atmospheric, and Planetary Sciences
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/jp0660987
