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J Biol Chem, Vol. 274, Issue 46, 32818-32828, November 12, 1999
From the Department of Molecular and Cell Biology and The Cancer
Research Laboratory, University of California,
Berkeley, California 94720-3200
In Con8 rat mammary epithelial tumor cells, the
synthetic glucocorticoid dexamethasone stimulates the remodeling of the
apical junction (tight and adherens junctions) and the transepithelial electrical resistance (TER), which reflects tight junction sealing. Indirect immunofluorescence revealed that dexamethasone induced the
recruitment of endogenous Ras and the p85 regulatory subunit of
phosphatidylinositol (PI) 3-kinase to regions of cell-cell contact,
concurrently with the stimulation of TER. Expression of
dominant-negative RasN17 abolished the dexamethasone stimulation in
TER, whereas, dexamethasone induced the reorganization of tight junction and adherens junction proteins, ZO-1 and 
-catenin, as well
as F-actin, to precise regions of cell-cell contact in a Ras-independent manner. Confocal microscopy revealed that RasN17 and
the p85 regulatory subunit of PI 3-kinase co-localized with ZO-1 and
F-actin at the tight junction and adherens junction, respectively.
Treatment with either of the PI 3-kinase inhibitors, wortmannin or
LY294002, or the MEK inhibitor PD 098059, which prevents MAPK
signaling, attenuated the dexamethasone stimulation of TER without
affecting apical junction remodeling. Similar to dominant-negative
RasN17, disruption of both Ras effector pathways using a combination of
inhibitors abolished the glucocorticoid stimulation of TER. Thus, the
glucocorticoiddependent remodeling of the apical junction and
tight junction sealing can be uncoupled by their dependence on Ras
and/or PI 3-kinase-dependent pathways, implicating a new
role for Ras and PI 3-kinase cell signaling events in the steroid
control of cell-cell interactions.
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