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Biophys J, June 2001, p. 2667-2677, Vol. 80, No. 6
and
*Kusumi Membrane Organizer Project, Exploratory Research for
Advanced Technology Organization, Japan Science and Technology
Corporation, Chiyoda 5-11-33, Nagoya 460-0012; and
Department of Biological Science, Nagoya University,
Nagoya 464-8602, Japan
Single green fluorescent protein (GFP) molecules were
successfully imaged for the first time in living cells. GFP linked to the cytoplasmic carboxyl terminus of E-cadherin (E-cad-GFP) was expressed in mouse fibroblast L cells, and observed using an
objective-type total internal reflection fluorescence microscope. Based
on the fluorescence intensity of individual fluorescent spots, the
majority of E-cad-GFP molecules on the free cell surface were found to be oligomers of various sizes, many of them greater than dimers, suggesting that oligomerization of E-cadherin takes place before its
assembly at cell-cell adhesion sites. The translational diffusion coefficient of E-cad-GFP is reduced by a factor of 10 to 40 upon oligomerization. Because such large decreases in translational mobility
cannot be explained solely by increases in radius upon oligomerization,
an oligomerization-induced trapping model is proposed in which, when
oligomers are formed, they are trapped in place due to greatly enhanced
tethering and corralling effects of the membrane skeleton on oligomers
(compared with monomers). The presence of many oligomers greater than
dimers on the free surface suggests that these greater oligomers are
the basic building blocks for the two-dimensional cell adhesion
structures (adherens junctions).
Biophys J, June 2001, p. 2667-2677, Vol. 80, No. 6
© 2001 by the Biophysical Society 0006-3495/01/06/2667/11 $2.00
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