Toward understanding the dynamics of membrane-raft-based molecular interactions.
The cell membrane is a 2-dimensional non-ideal liquid containing dynamic structures on various time-space scales, and the raft domain is one of them. Existing literature supports the concept that raft dynamics may be important for its formation and function: the raft function may be supported by stimulation-induced raft association/coalescence and recruitment of various raftophilic molecules to coalesced rafts, and, importantly, they both may happen transiently. Thus, one must always consider the limited association time of a raft or a raftophilic molecule with another raft, even when one interprets the results of static experiments, such as immunofluorescence and pull-down assays. Critical considerations on the chemical fixation mechanism and immunocolocalization data suggest that the temporary nature of raft-based molecular interactions may explain why colocalization results are sensitive to subtle variations in experimental conditions employed in different laboratories.
Kusumi
Akihiro
A
The Institute for Frontier Medical Sciences, Kyoto University, 606-8507, Japan. akusumi@frontier.kyoto-u.ac.jp
Suzuki
Kenichi
K
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D003432:Cross-Linking Reagents; D003902:Detergents; D004058:Diffusion; D005404:Fixatives; D005455:Fluorescent Antibody Technique / Q000379:methods; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D006801:Humans; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000378:metabolism*; D021962:Membrane Microdomains / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological
D003432:Cross-Linking Reagents; D003902:Detergents; D005404:Fixatives; D017261:Glycosylphosphatidylinositols; D008563:Membrane Lipids; D008565:Membrane Proteins