The function of cingulin is presently not fully understood, but the cingulin protein has been reported to be present in tight junctions interacting with the tight junction protein ZO-1 [ 49].
Despite its typical location below tight junctions, it interacts with several bacteria, facilitating internalization and colonization.
Indeed, in epithelial cells, ZO-1 is concentrated in tight junctions, where it interacts with integral transmembrane proteins including occludin, claudins and JAMs (junctional adhesion molecules), which are specifically enriched at this type of junctions.
From the amplitude displacement data, three-dimensional surface contour plots of the wave energy are generated to find out how the elastic energy interacts with the tight fatigue crack interfaces.
Therefore, in response to claudin disruption, claudin and occludin move out of the tight junction and interact with the key protein components of the intrinsic apoptotic signaling pathway.
PARD3 is a member of a family of adaptor proteins playing a central role in the formation of epithelial tight junctions by interacting with other members of the PARD family of proteins [ 40].
It was recently shown that microtubules contribute to the mechanism of cell detachment through TBCD by transporting it to the cell membrane where it interacts with adherent and tight junctions [ 16].
Earlier, it was shown that the dimeric 14-3-3γ 14-3-3γ 14-3-3γphosphorylated HspB6 but interacts to form tight complexes with unphosphorylated HspB6 or its phosphomimicking mutant, S16D.
Furthermore, recent data demonstrated that EpCAM interacts with proteins of the claudin family and fosters tight junction formation and actomyosin-dependent contractility (84, 85).
Instead of binding with Ub, USP53 interacts with ZO-1 and ZO-2 as a part of the tight junction complex (Kazmierczak et al., 2015).
