Cingulin was originally discovered at the MRC Laboratory of Molecular Biology (Cambridge, UK) by Dr. Sandra Citi, as a protein present in chicken intestinal epithelial cells, that co-purified with non-muscle myosin II and was specifically localized at tight junctions (zonulae occludentes).

In vitro, cingulin can bind to and bundle actin filaments, and interact with myosin II and several TJ proteins including ZO-1, ZO-2, ZO-3, paracingulin and occludin.

Embryoid bodies derived from embryonic stem cells where one or both cingulin alleles were targeted by homologous recombination show apparently normal tight junctions, but changes in the expression of a large number of genes, including tight junction protein genes (claudin-2, claudin-6, claudin-7 and occludin) and transcription factors (including GATA4).

Furthermore, the synthesis of cingulin in early mouse embryos is tissue-specific and it occurs in blastocyst (up-regulated in trophectoderm and down-regulated in inner-cells).

[22][23] In Xenopus laevis embryos, maternal cingulin is recruited to apical cell-cell junctions from 2-cells stage.