Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase

2005 ◽  
Vol 2 (2) ◽  
pp. 99-104 ◽  
Author(s):  
Irwin Chen ◽  
Mark Howarth ◽  
Weiying Lin ◽  
Alice Y Ting
2019 ◽  
Vol 14 (8) ◽  
pp. 1836-1844 ◽  
Author(s):  
Ross W. Cheloha ◽  
Zeyang Li ◽  
Djenet Bousbaine ◽  
Andrew W. Woodham ◽  
Priscillia Perrin ◽  
...  

Author(s):  
Watt W. Webb

Plasma membrane heterogeneity is implicit in the existence of specialized cell surface organelles which are necessary for cellular function; coated pits, post and pre-synaptic terminals, microvillae, caveolae, tight junctions, focal contacts and endothelial polarization are examples. The persistence of these discrete molecular aggregates depends on localized restraint of the constituent molecules within specific domaines in the cell surface by strong intermolecular bonds and/or anchorage to extended cytoskeleton. The observed plasticity of many of organelles and the dynamical modulation of domaines induced by cellular signaling evidence evanescent intermolecular interactions even in conspicuous aggregates. There is also strong evidence that universal restraints on the mobility of cell surface proteins persist virtually everywhere in cell surfaces, not only in the discrete organelles. Diffusion of cell surface proteins is slowed by several orders of magnitude relative to corresponding protein diffusion coefficients in isolated lipid membranes as has been determined by various ensemble average methods of measurement such as fluorescence photobleaching recovery(FPR).


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