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Title: Modeling the Membrane Environment for Membrane Proteins
Award ID(s):
0832571
NSF-PAR ID:
10021136
Author(s) / Creator(s):
; ; ; ;
Date Published:
Journal Name:
Biophysical Journal
Volume:
100
Issue:
8
ISSN:
0006-3495
Page Range / eLocation ID:
2073 to 2074
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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  1. Several groups have recently reported evidence for the emergence of domains in cell plasma membranes when membrane proteins are organized by ligand binding or assembly of membrane proximal scaffolds. These domains recruit and retain components that favor the liquid-ordered phase, adding to a decades-old literature interrogating the contribution of membrane phase separation in plasma membrane organization and function. Here we propose that both past and present observations are consistent with a model in which membranes have a high compositional susceptibility, arising from their thermodynamic state in a single phase that is close to a miscibility phase transition. This rigorous framework naturally allows for both transient structure in the form of composition fluctuations and long-lived structure in the form of induced domains. In this way, the biological tuning of plasma membrane composition enables a responsive compositional landscape that facilitates and augments cellular biochemistry vital to plasma membrane functions. 
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