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Vol. 13, Issue 4, 1227-1237, April 2002
*Department of Anatomy and Cell Biology, East Carolina University
School of Medicine, Greenville, North Carolina 27858; and
§Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115
Occludin is an integral membrane protein that is tyrosine
phosphorylated when localized at tight junctions. When Ca2+
was depleted from the culture medium, occludin tyrosine phosphorylation was diminished from Madin-Darby canine kidney epithelial cells in 2 min. This dephosphorylation was correlated with a significant reduction in transepithelial electrical resistance (TER), indicating a
global loss of the tight junction barrier function. Reconstitution of
Ca2+ resulted in a robust tyrosine rephosphorylation of
occludin that was temporally associated with an increase in TER.
Moreover, we demonstrate in this study that occludin was colocalized
with the nonreceptor tyrosine kinase c-Yes at cell junction areas and
formed an immunoprecipitable complex with c-Yes in vivo. This complex dissociated when the cells were incubated in medium without
Ca2+ or treated with a c-Yes inhibitor, CGP77675. In
the presence of CGP77675 after Ca2+ repletion, occludin
tyrosine phosphorylation was completely abolished and both tight
junction formation and the increase of the TER were inhibited. Our
study thus provides strong evidence that occludin tyrosine
phosphorylation is tightly linked to tight junction formation in
epithelial cells, and that the nonreceptor tyrosine kinase c-Yes is
involved in the regulation of this process.
Corresponding author. E-mail address:
cheny{at}mail.ecu.edu.
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