[HTML][HTML] Protein interactions at the tight junction: actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
ES Wittchen, J Haskins, BR Stevenson - Journal of Biological Chemistry, 1999 - ASBMB
Defining how the molecular constituents of the tight junction interact is a prerequisite to
understanding tight junction physiology. We utilized in vitro binding assays with purified
recombinant proteins and immunoprecipitation analyses to define interactions between ZO-
1, ZO-2, ZO-3, occludin, and the actin cytoskeleton. Actin cosedimentation studies showed
that ZO-2, ZO-3, and occludin all interact directly with F-actin in vitro, indicating that actin is
engaged in multiple interactions at the tight junction. Low speed sedimentation analyses …
understanding tight junction physiology. We utilized in vitro binding assays with purified
recombinant proteins and immunoprecipitation analyses to define interactions between ZO-
1, ZO-2, ZO-3, occludin, and the actin cytoskeleton. Actin cosedimentation studies showed
that ZO-2, ZO-3, and occludin all interact directly with F-actin in vitro, indicating that actin is
engaged in multiple interactions at the tight junction. Low speed sedimentation analyses …