10.1021/acsnano.5b07595.s005
Ignacio Munguira
Ignacio
Munguira
Ignacio Casuso
Ignacio
Casuso
Hirohide Takahashi
Hirohide
Takahashi
Felix Rico
Felix
Rico
Atsushi Miyagi
Atsushi
Miyagi
Mohamed Chami
Mohamed
Chami
Simon Scheuring
Simon
Scheuring
Glasslike
Membrane Protein Diffusion in a Crowded
Membrane
American Chemical Society
2016
Glasslike Membrane Protein Diffusion
document coexistence
novel analysis methodology
membrane diffusion
plasma membrane
observation capabilities
Crowded MembraneMany functions
protein lysenin
force microscopy
immobile molecules
diffusion regimes
time scales
fluid bilayer
glass phase
fluorescence microscopy
2016-02-09 00:00:00
Dataset
https://acs.figshare.com/articles/dataset/Glasslike_Membrane_Protein_Diffusion_in_a_Crowded_Membrane/2087782
Many
functions of the plasma membrane depend critically on its
structure and dynamics. Observation of anomalous diffusion <i>in vivo</i> and <i>in vitro</i> using fluorescence
microscopy and single particle tracking has advanced our concept of the membrane from a homogeneous
fluid bilayer with freely diffusing proteins to a highly organized
crowded and clustered mosaic of lipids and proteins. Unfortunately,
anomalous diffusion could not be related to local molecular details
given the lack of direct and unlabeled molecular observation capabilities.
Here, we use high-speed atomic force microscopy and a novel analysis
methodology to analyze the pore forming protein lysenin in a highly
crowded environment and document coexistence of several diffusion
regimes within one membrane. We show the formation of local glassy
phases, where proteins are trapped in neighbor-formed cages for time
scales up to 10 s, which had not been previously experimentally reported
for biological membranes. Furthermore, around solid-like patches and
immobile molecules a slower glass phase is detected leading to protein
trapping and creating a perimeter of decreased membrane diffusion.